STRINGSTRING
XP_444937.1 protein (Candida glabrata) - STRING interaction network
"XP_444937.1" - Hypothetical protein in Candida glabrata
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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:
some 3D structure is known or predicted
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Edges represent protein-protein associations
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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
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
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[Homology]
Score
XP_444937.1Hypothetical protein (437 aa)    
Predicted Functional Partners:
XP_447089.1
Hypothetical protein (180 aa)
     
 
  0.634
XP_448981.1
Hypothetical protein (374 aa)
       
 
  0.631
XP_447392.1
Hypothetical protein (646 aa)
     
      0.609
XP_447319.1
Hypothetical protein (647 aa)
     
      0.609
COX2
Cytochrome-c oxidase subunit II; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1- 3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1 (227 aa)
       
 
  0.578
COX1
Cytochrome-c oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1- 3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B (534 aa)
       
 
  0.549
mge1
Hypothetical protein; Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of SSC1 to substrate proteins (By similarity) (231 aa)
     
      0.535
COX10
Hypothetical protein; Converts protoheme IX and farnesyl diphosphate to heme O (451 aa)
     
 
  0.525
ATP9
ATP synthase protein 9; Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subuni [...] (76 aa)
     
 
  0.523
XP_448692.1
Hypothetical protein (67 aa)
       
 
  0.511
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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