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ATP1A3 protein (human) - STRING interaction network
"ATP1A3" - Sodium/potassium-transporting ATPase subunit alpha-3 in Homo sapiens
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
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gene co-occurrence
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textmining
co-expression
protein homology
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ATP1A3Sodium/potassium-transporting ATPase subunit alpha-3; This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients; Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily (1026 aa)    
Predicted Functional Partners:
ATP1B3
Sodium/potassium-transporting ATPase subunit beta-3; This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-3 subunit is not known; ATPase Na+/K+ transporting subunits (279 aa)
     
  0.994
ATP1B1
Sodium/potassium-transporting ATPase subunit beta-1; This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane; ATPase Na+/K+ transporting subunits (303 aa)
     
  0.990
ATP1B2
Sodium/potassium-transporting ATPase subunit beta-2; This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-2 subunit is not known; ATPase Na+/K+ transporting subunits (290 aa)
     
  0.978
FXYD2
Sodium/potassium-transporting ATPase subunit gamma; May be involved in forming the receptor site for cardiac glycoside binding or may modulate the transport function of the sodium ATPase; Belongs to the FXYD family (66 aa)
     
  0.970
ATP1B4
Protein ATP1B4; May act as a transcriptional coregulator during muscle development through its interaction with SNW1. Has lost its ancestral function as a Na,K-ATPase beta-subunit; Belongs to the X(+)/potassium ATPases subunit beta family (357 aa)
     
  0.939
FXYD7
FXYD domain containing ion transport regulator 7; Belongs to the FXYD family (80 aa)
     
 
  0.937
FXYD6
FXYD domain containing ion transport regulator 6; Belongs to the FXYD family (144 aa)
     
 
  0.931
RS1
Retinoschisin; Binds negatively charged membrane lipids, such as phosphatidylserine and phosphoinositides (By similarity). May play a role in cell-cell adhesion processes in the retina, via homomeric interaction between octamers present on the surface of two neighboring cells. Required for normal structure and function of the retina (224 aa)
     
 
  0.924
FXYD1
Phospholemman; Associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which transports Na(+) out of the cell and K(+) into the cell. Inhibits NKA activity in its unphosphorylated state and stimulates activity when phosphorylated. Reduces glutathionylation of the NKA beta-1 subunit ATP1B1, thus reversing glutathionylation-mediated inhibition of ATP1B1. Contributes to female sexual development by maintaining the excitability of neurons which secrete gonadotropin-releasing hormone (92 aa)
     
 
  0.914
FXYD3
FXYD domain-containing ion transport regulator 3; Associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which transports Na(+) out of the cell and K(+) into the cell. Reduces glutathionylation of the NKA beta-1 subunit ATP1B1, thus reversing glutathionylation-mediated inhibition of ATP1B1. Induces a hyperpolarization-activated chloride current when expressed in Xenopus oocytes (144 aa)
         
  0.912
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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