SLC4A1 protein (human) - STRING database

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SLC4A1

Band 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

0.939

ALAS2

0.905

GYPA

0.873

AHSP

0.866

EPB41

0.845

GYPB

0.834

ANK1

0.827

CA1

0.805

HBD

0.748

SELENBP1

0.737

Your Current Organism:

Homo sapiens

NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
AHSP	ALAS2	ENSP00000307199	ENSP00000332369	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	5-aminolevulinate synthase, erythroid-specific, mitochondrial; 5’-aminolevulinate synthase 2	0.920
AHSP	CA1	ENSP00000307199	ENSP00000430656	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	Carbonic anhydrase 1; Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea; Carbonic anhydrases	0.789
AHSP	EPB42	ENSP00000307199	ENSP00000300215	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	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	0.900
AHSP	GYPA	ENSP00000307199	ENSP00000354003	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	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 [...]	0.458
AHSP	GYPB	ENSP00000307199	ENSP00000427690	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	Glycophorin-B; This protein is a minor sialoglycoprotein in erythrocyte membranes; Belongs to the glycophorin-A family	0.792
AHSP	HBD	ENSP00000307199	ENSP00000369654	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	Hemoglobin subunit delta; Involved in oxygen transport from the lung to the various peripheral tissues; Belongs to the globin family	0.963
AHSP	SELENBP1	ENSP00000307199	ENSP00000397261	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	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)	0.631
AHSP	SLC4A1	ENSP00000307199	ENSP00000262418	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	Band 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 [...]	0.866
ALAS2	AHSP	ENSP00000332369	ENSP00000307199	5-aminolevulinate synthase, erythroid-specific, mitochondrial; 5’-aminolevulinate synthase 2	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	0.920
ALAS2	ANK1	ENSP00000332369	ENSP00000265709	5-aminolevulinate synthase, erythroid-specific, mitochondrial; 5’-aminolevulinate synthase 2	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	0.444
ALAS2	CA1	ENSP00000332369	ENSP00000430656	5-aminolevulinate synthase, erythroid-specific, mitochondrial; 5’-aminolevulinate synthase 2	Carbonic anhydrase 1; Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea; Carbonic anhydrases	0.753
ALAS2	EPB42	ENSP00000332369	ENSP00000300215	5-aminolevulinate synthase, erythroid-specific, mitochondrial; 5’-aminolevulinate synthase 2	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	0.918
ALAS2	GYPA	ENSP00000332369	ENSP00000354003	5-aminolevulinate synthase, erythroid-specific, mitochondrial; 5’-aminolevulinate synthase 2	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 [...]	0.550
ALAS2	GYPB	ENSP00000332369	ENSP00000427690	5-aminolevulinate synthase, erythroid-specific, mitochondrial; 5’-aminolevulinate synthase 2	Glycophorin-B; This protein is a minor sialoglycoprotein in erythrocyte membranes; Belongs to the glycophorin-A family	0.788
ALAS2	HBD	ENSP00000332369	ENSP00000369654	5-aminolevulinate synthase, erythroid-specific, mitochondrial; 5’-aminolevulinate synthase 2	Hemoglobin subunit delta; Involved in oxygen transport from the lung to the various peripheral tissues; Belongs to the globin family	0.846
ALAS2	SELENBP1	ENSP00000332369	ENSP00000397261	5-aminolevulinate synthase, erythroid-specific, mitochondrial; 5’-aminolevulinate synthase 2	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)	0.582
ALAS2	SLC4A1	ENSP00000332369	ENSP00000262418	5-aminolevulinate synthase, erythroid-specific, mitochondrial; 5’-aminolevulinate synthase 2	Band 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 [...]	0.905
ANK1	ALAS2	ENSP00000265709	ENSP00000332369	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	5-aminolevulinate synthase, erythroid-specific, mitochondrial; 5’-aminolevulinate synthase 2	0.444
ANK1	EPB41	ENSP00000265709	ENSP00000345259	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	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	0.663
ANK1	EPB42	ENSP00000265709	ENSP00000300215	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	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	0.775

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