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PSY2 protein (Candida glabrata) - STRING interaction network
"PSY2" - Hypothetical protein in Candida glabrata
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query proteins and first shell of interactors
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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
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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PSY2Hypothetical 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)    
Predicted Functional Partners:
PSY4
Hypothetical protein; 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) (402 aa)
       
  0.934
PPH3
Hypothetical 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)
       
  0.911
XP_448668.1
Hypothetical protein (917 aa)
     
      0.893
SPT5
Hypothetical protein; The SPT4-SPT5 complex mediates both activation and inhibition of transcription elongation, and plays a role in pre- mRNA processing. This complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene (By similarity) (1010 aa)
     
      0.833
RRD1
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) (424 aa)
       
 
  0.813
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)
       
  0.708
XP_448282.1
Hypothetical protein (325 aa)
       
 
  0.688
XP_449816.1
Hypothetical protein (364 aa)
       
 
  0.615
PPH21
Hypothetical protein (368 aa)
       
 
  0.615
XP_448441.1
Hypothetical protein (320 aa)
       
 
  0.614
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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