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SLC4A1 protein (human) - STRING interaction network
"SLC4A1" - Band 3 anion transport protein in Homo sapiens
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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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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SLC4A1Band 3 anion transport protein; Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Major integral membrane glycoprotein of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin. Functions as a transporter that mediates the 1-1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate excha [...] (911 aa)    
Predicted Functional Partners:
EPB42
Erythrocyte membrane protein band 4.2; Probably plays an important role in the regulation of erythrocyte shape and mechanical properties; Belongs to the transglutaminase superfamily. Transglutaminase family (721 aa)
     
 
  0.939
ALAS2
5-aminolevulinate synthase, erythroid-specific, mitochondrial; 5’-aminolevulinate synthase 2 (587 aa)
     
   
  0.905
GYPA
Glycophorin-A; Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for [...] (150 aa)
     
 
  0.873
AHSP
Alpha-hemoglobin-stabilizing protein; Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia; Belongs to the AHSP family (102 aa)
     
   
  0.866
EPB41
Protein 4.1; Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase (864 aa)
     
 
  0.845
GYPB
Glycophorin-B; This protein is a minor sialoglycoprotein in erythrocyte membranes; Belongs to the glycophorin-A family (91 aa)
     
   
  0.834
ANK1
Ankyrin-1; Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions (1897 aa)
     
 
  0.827
CA1
Carbonic anhydrase 1; Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea; Carbonic anhydrases (261 aa)
     
 
  0.805
HBD
Hemoglobin subunit delta; Involved in oxygen transport from the lung to the various peripheral tissues; Belongs to the globin family (147 aa)
     
   
  0.748
SELENBP1
Selenium-binding protein 1; Selenium-binding protein which may be involved in the sensing of reactive xenobiotics in the cytoplasm. May be involved in intra-Golgi protein transport (By similarity) (514 aa)
     
   
  0.737
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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