Details for: SLC4A1

Gene ID: 6521

Symbol: SLC4A1

Ensembl ID: ENSG00000004939

Description: solute carrier family 4 member 1 (Diego blood group)

Associated with

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: basophilic erythroblast (CL0000549)
    Fold Change: 36.4071
    Cell Significance Index: 16.5800
  • Cell Name: columnar/cuboidal epithelial cell (CL0000075)
    Fold Change: 20.8619
    Cell Significance Index: 79.8800
  • Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
    Fold Change: 9.4621
    Cell Significance Index: -2.4000
  • Cell Name: mucosal type mast cell (CL0000485)
    Fold Change: 5.5507
    Cell Significance Index: -2.2600
  • Cell Name: proerythroblast (CL0000547)
    Fold Change: 3.5540
    Cell Significance Index: 50.9300
  • Cell Name: primitive red blood cell (CL0002355)
    Fold Change: 0.7460
    Cell Significance Index: 8.4500
  • Cell Name: enucleate erythrocyte (CL0000595)
    Fold Change: 0.7173
    Cell Significance Index: 3.7100
  • Cell Name: reticulocyte (CL0000558)
    Fold Change: 0.7091
    Cell Significance Index: 3.7300
  • Cell Name: stromal cell of bone marrow (CL0010001)
    Fold Change: 0.6513
    Cell Significance Index: -2.5700
  • Cell Name: transit amplifying cell of colon (CL0009011)
    Fold Change: 0.5273
    Cell Significance Index: 16.8900
  • Cell Name: medial ganglionic eminence derived interneuron (CL4023063)
    Fold Change: 0.1473
    Cell Significance Index: 2.1100
  • Cell Name: cerebellar granule cell (CL0001031)
    Fold Change: 0.1255
    Cell Significance Index: 2.1500
  • Cell Name: eye photoreceptor cell (CL0000287)
    Fold Change: 0.0708
    Cell Significance Index: 4.4600
  • Cell Name: hepatoblast (CL0005026)
    Fold Change: 0.0553
    Cell Significance Index: 0.9300
  • Cell Name: neoplastic cell (CL0001063)
    Fold Change: 0.0382
    Cell Significance Index: 7.5900
  • Cell Name: intermediate cell of urothelium (CL4030055)
    Fold Change: 0.0232
    Cell Significance Index: 4.1800
  • Cell Name: odontoblast (CL0000060)
    Fold Change: 0.0154
    Cell Significance Index: 1.9800
  • Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
    Fold Change: 0.0131
    Cell Significance Index: 2.6200
  • Cell Name: abnormal cell (CL0001061)
    Fold Change: 0.0125
    Cell Significance Index: 1.2800
  • Cell Name: kidney collecting duct intercalated cell (CL1001432)
    Fold Change: 0.0116
    Cell Significance Index: 0.1100
  • Cell Name: early T lineage precursor (CL0002425)
    Fold Change: 0.0110
    Cell Significance Index: 0.1600
  • Cell Name: decidual cell (CL2000002)
    Fold Change: 0.0075
    Cell Significance Index: 0.1200
  • Cell Name: skeletal muscle fibroblast (CL0011027)
    Fold Change: 0.0058
    Cell Significance Index: 0.0400
  • Cell Name: dopaminergic neuron (CL0000700)
    Fold Change: 0.0057
    Cell Significance Index: 1.6500
  • Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
    Fold Change: 0.0017
    Cell Significance Index: 0.6000
  • Cell Name: bladder urothelial cell (CL1001428)
    Fold Change: 0.0013
    Cell Significance Index: 0.0700
  • Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
    Fold Change: 0.0007
    Cell Significance Index: 0.0200
  • Cell Name: mesothelial cell of epicardium (CL0011019)
    Fold Change: 0.0000
    Cell Significance Index: 0.0000
  • Cell Name: pigmented epithelial cell (CL0000529)
    Fold Change: -0.0002
    Cell Significance Index: -0.3000
  • Cell Name: anterior lens cell (CL0002223)
    Fold Change: -0.0004
    Cell Significance Index: -0.7300
  • Cell Name: lens epithelial cell (CL0002224)
    Fold Change: -0.0013
    Cell Significance Index: -1.9600
  • Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
    Fold Change: -0.0019
    Cell Significance Index: -1.4300
  • Cell Name: secondary lens fiber (CL0002225)
    Fold Change: -0.0021
    Cell Significance Index: -2.8900
  • Cell Name: pancreatic A cell (CL0000171)
    Fold Change: -0.0030
    Cell Significance Index: -2.1900
  • Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
    Fold Change: -0.0031
    Cell Significance Index: -1.9500
  • Cell Name: cell in vitro (CL0001034)
    Fold Change: -0.0031
    Cell Significance Index: -1.7000
  • Cell Name: pulmonary alveolar epithelial cell (CL0000322)
    Fold Change: -0.0032
    Cell Significance Index: -2.4200
  • Cell Name: hair follicular keratinocyte (CL2000092)
    Fold Change: -0.0034
    Cell Significance Index: -1.5200
  • Cell Name: type B pancreatic cell (CL0000169)
    Fold Change: -0.0039
    Cell Significance Index: -2.2200
  • Cell Name: ciliary muscle cell (CL1000443)
    Fold Change: -0.0049
    Cell Significance Index: -2.2300
  • Cell Name: lung endothelial cell (CL1001567)
    Fold Change: -0.0049
    Cell Significance Index: -0.2600
  • Cell Name: pancreatic acinar cell (CL0002064)
    Fold Change: -0.0056
    Cell Significance Index: -0.9600
  • Cell Name: pigmented ciliary epithelial cell (CL0002303)
    Fold Change: -0.0061
    Cell Significance Index: -0.8900
  • Cell Name: renal alpha-intercalated cell (CL0005011)
    Fold Change: -0.0083
    Cell Significance Index: -0.0800
  • Cell Name: pancreatic D cell (CL0000173)
    Fold Change: -0.0108
    Cell Significance Index: -2.2700
  • Cell Name: basal cell of urothelium (CL1000486)
    Fold Change: -0.0120
    Cell Significance Index: -1.4700
  • Cell Name: epithelial cell of stomach (CL0002178)
    Fold Change: -0.0135
    Cell Significance Index: -1.5700
  • Cell Name: pancreatic ductal cell (CL0002079)
    Fold Change: -0.0144
    Cell Significance Index: -1.6500
  • Cell Name: lactocyte (CL0002325)
    Fold Change: -0.0154
    Cell Significance Index: -2.0000
  • Cell Name: stromal cell of ovary (CL0002132)
    Fold Change: -0.0164
    Cell Significance Index: -2.2500
  • Cell Name: erythrocyte (CL0000232)
    Fold Change: -0.0169
    Cell Significance Index: -0.4300
  • Cell Name: acinar cell of salivary gland (CL0002623)
    Fold Change: -0.0180
    Cell Significance Index: -0.8400
  • Cell Name: erythroblast (CL0000765)
    Fold Change: -0.0189
    Cell Significance Index: -0.2300
  • Cell Name: forebrain neuroblast (CL1000042)
    Fold Change: -0.0205
    Cell Significance Index: -1.2600
  • Cell Name: sebum secreting cell (CL0000317)
    Fold Change: -0.0206
    Cell Significance Index: -1.4600
  • Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
    Fold Change: -0.0245
    Cell Significance Index: -1.8300
  • Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
    Fold Change: -0.0247
    Cell Significance Index: -2.5700
  • Cell Name: helper T cell (CL0000912)
    Fold Change: -0.0250
    Cell Significance Index: -0.3600
  • Cell Name: transit amplifying cell of small intestine (CL0009012)
    Fold Change: -0.0251
    Cell Significance Index: -0.5200
  • Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
    Fold Change: -0.0273
    Cell Significance Index: -2.1700
  • Cell Name: tonsil germinal center B cell (CL2000006)
    Fold Change: -0.0297
    Cell Significance Index: -3.5000
  • Cell Name: hippocampal granule cell (CL0001033)
    Fold Change: -0.0314
    Cell Significance Index: -2.1100
  • Cell Name: cardiac muscle myoblast (CL0000513)
    Fold Change: -0.0329
    Cell Significance Index: -2.5300
  • Cell Name: eukaryotic cell (CL0000255)
    Fold Change: -0.0338
    Cell Significance Index: -1.4700
  • Cell Name: early pro-B cell (CL0002046)
    Fold Change: -0.0350
    Cell Significance Index: -2.2600
  • Cell Name: enterocyte of epithelium of large intestine (CL0002071)
    Fold Change: -0.0353
    Cell Significance Index: -1.6000
  • Cell Name: glycinergic neuron (CL1001509)
    Fold Change: -0.0358
    Cell Significance Index: -1.8800
  • Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
    Fold Change: -0.0367
    Cell Significance Index: -1.7300
  • Cell Name: intestinal tuft cell (CL0019032)
    Fold Change: -0.0369
    Cell Significance Index: -2.2600
  • Cell Name: cortical cell of adrenal gland (CL0002097)
    Fold Change: -0.0381
    Cell Significance Index: -1.0200
  • Cell Name: renal intercalated cell (CL0005010)
    Fold Change: -0.0401
    Cell Significance Index: -0.3200
  • Cell Name: basal cell of prostate epithelium (CL0002341)
    Fold Change: -0.0443
    Cell Significance Index: -1.2100
  • Cell Name: glandular cell of esophagus (CL0002657)
    Fold Change: -0.0448
    Cell Significance Index: -0.4800
  • Cell Name: retinal progenitor cell (CL0002672)
    Fold Change: -0.0470
    Cell Significance Index: -2.6400
  • Cell Name: endothelial cell of venule (CL1000414)
    Fold Change: -0.0475
    Cell Significance Index: -0.5400
  • Cell Name: epithelial cell of proximal tubule (CL0002306)
    Fold Change: -0.0484
    Cell Significance Index: -0.3700
  • Cell Name: fibroblast of dermis (CL0002551)
    Fold Change: -0.0506
    Cell Significance Index: -1.0600
  • Cell Name: preadipocyte (CL0002334)
    Fold Change: -0.0507
    Cell Significance Index: -0.9900
  • Cell Name: skeletal muscle fiber (CL0008002)
    Fold Change: -0.0517
    Cell Significance Index: -1.3300
  • Cell Name: L5 extratelencephalic projecting glutamatergic cortical neuron (CL4023041)
    Fold Change: -0.0537
    Cell Significance Index: -1.8800
  • Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
    Fold Change: -0.0557
    Cell Significance Index: -1.9400
  • Cell Name: L6b glutamatergic cortical neuron (CL4023038)
    Fold Change: -0.0571
    Cell Significance Index: -1.8700
  • Cell Name: kidney collecting duct principal cell (CL1001431)
    Fold Change: -0.0582
    Cell Significance Index: -0.5300
  • Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
    Fold Change: -0.0584
    Cell Significance Index: -1.8600
  • Cell Name: kidney epithelial cell (CL0002518)
    Fold Change: -0.0598
    Cell Significance Index: -1.7600
  • Cell Name: cytotoxic T cell (CL0000910)
    Fold Change: -0.0611
    Cell Significance Index: -0.8900
  • Cell Name: CD4-positive, alpha-beta thymocyte (CL0000810)
    Fold Change: -0.0621
    Cell Significance Index: -1.0700
  • Cell Name: indirect pathway medium spiny neuron (CL4023029)
    Fold Change: -0.0624
    Cell Significance Index: -2.7600
  • Cell Name: neutrophil progenitor cell (CL0000834)
    Fold Change: -0.0630
    Cell Significance Index: -1.6900
  • Cell Name: pro-T cell (CL0000827)
    Fold Change: -0.0646
    Cell Significance Index: -1.6500
  • Cell Name: placental villous trophoblast (CL2000060)
    Fold Change: -0.0659
    Cell Significance Index: -1.7600
  • Cell Name: erythroid lineage cell (CL0000764)
    Fold Change: -0.0671
    Cell Significance Index: -0.7400
  • Cell Name: kidney capillary endothelial cell (CL1000892)
    Fold Change: -0.0676
    Cell Significance Index: -0.7000
  • Cell Name: epithelial cell of uterus (CL0002149)
    Fold Change: -0.0677
    Cell Significance Index: -0.9400
  • Cell Name: keratocyte (CL0002363)
    Fold Change: -0.0681
    Cell Significance Index: -1.0800
  • Cell Name: direct pathway medium spiny neuron (CL4023026)
    Fold Change: -0.0726
    Cell Significance Index: -2.7500
  • Cell Name: lens fiber cell (CL0011004)
    Fold Change: -0.0734
    Cell Significance Index: -2.3200
  • Cell Name: near-projecting glutamatergic cortical neuron (CL4023012)
    Fold Change: -0.0738
    Cell Significance Index: -1.8400
  • Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
    Fold Change: -0.0755
    Cell Significance Index: -1.4000
  • Cell Name: conjunctival epithelial cell (CL1000432)
    Fold Change: -0.0755
    Cell Significance Index: -1.0300

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Other Information

**Key Characteristics:** 1. **Bicarbonate Transporter:** The SLC4A1 gene encodes for the Anion exchange protein 1 (B3AT_HUMAN), a bicarbonate transporter responsible for the uptake and release of bicarbonate ions in various tissues. 2. **Membrane-Bound Protein:** The B3AT_HUMAN protein is a transmembrane protein, with its extracellular and cytoplasmic domains interacting with other proteins to regulate its activity. 3. **Regulation of pH:** The SLC4A1 gene plays a critical role in maintaining acid-base balance in the body by regulating the uptake and release of bicarbonate ions. 4. **Expression in Various Tissues:** The SLC4A1 gene is expressed in multiple tissues, including the kidneys, erythrocytes, epithelial cells, and immune cells. **Pathways and Functions:** 1. **Bicarbonate Transport:** The SLC4A1 gene regulates the transport of bicarbonate ions across cell membranes, influencing pH homeostasis and acid-base balance. 2. **Ankyrin-1 Complex:** The B3AT_HUMAN protein interacts with ankyrin-1, a cytoskeletal protein that regulates the stability and function of the erythrocyte membrane. 3. **Regulation of Glycolytic Process:** The SLC4A1 gene negatively regulates the glycolytic process through fructose-6-phosphate, influencing energy metabolism and glucose homeostasis. 4. **Regulation of Urine Volume:** The SLC4A1 gene regulates the volume of urine produced by the kidneys, influencing water balance and electrolyte homeostasis. **Clinical Significance:** 1. **Hereditary Spherocytosis Type 4 (HSP4):** Mutations in the SLC4A1 gene have been associated with HSP4, a rare genetic disorder characterized by spherocytic red blood cells and hemolytic anemia. 2. **Distal Renal Tubular Acidosis (dRTA):** The SLC4A1 gene is also associated with dRTA, a kidney disorder characterized by impaired bicarbonate reabsorption and acid-base disturbances. 3. **dRTA-Hemolytic Anemia (dRTA-HA):** Mutations in the SLC4A1 gene can also lead to dRTA-HA, a severe kidney disorder characterized by hemolytic anemia and acid-base disturbances. 4. **Implications for Clinical Management:** Understanding the role of the SLC4A1 gene in human disease can inform the development of targeted therapies for patients with hereditary spherocytosis, dRTA, and dRTA-HA. In conclusion, the SLC4A1 gene plays a critical role in regulating bicarbonate transport and maintaining acid-base balance in the human body. Mutations in this gene have been associated with several human diseases, including hereditary spherocytosis, distal renal tubular acidosis, and dRTA-hemolytic anemia. Further research into the mechanisms of SLC4A1 function and its role in human disease can inform the development of targeted therapies for patients with these disorders.

Genular Protein ID: 3081536412

Symbol: B3AT_HUMAN

Name: Anion exchange protein 1

UniProtKB Accession Codes:

P02730 G4V2I6 P78487 Q1ZZ45 Q4KKW9 Q4VB84 Q9UCY7 Q9UDJ1

Database IDs:

ABCD 1 AGR 1 AlphaFoldDB 1 Antibodypedia 1 Bgee 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 1 CORUM 1 CTD 1 ChEBI 2 ChiTaRS 1 DIP 1 DMDM 1 DNASU 1 DisGeNET 1 DisProt 1 ELM 1 EMBL 14 EMDB 38 Ensembl 1 EvolutionaryTrace 1 ExpressionAtlas 1 GO 32 Gene3D 1 GeneCards 1 GeneReviews 1 GeneTree 1 GeneWiki 1 GenomeRNAi 1 GlyConnect 1 GlyCosmos 1 GlyGen 1 HGNC 1 HOGENOM 1 HPA 1 InParanoid 1 IntAct 1 InterPro 7 KEGG 1 MANE-Select 1 MIM 19 MINT 1 MalaCards 1 MassIVE 1 MoonDB 1 MoonProt 1 NCBI Taxonomy 1 NCBIfam 1 OMA 1 OpenTargets 1 Orphanet 6 OrthoDB 1 PANTHER 2 PDB 51 PDBsum 51 PIR 1 PRINTS 3 PRO 1 PROSITE 2 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 2 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 1 RNAct 1 Reactome 4 RefSeq 2 Rhea 1 SIGNOR 1 SMR 1 STRING 1 SUPFAM 1 SignaLink 1 SwissPalm 1 TCDB 1 TreeFam 1 UCSC 1 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 3223947

Title: The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequence.

PubMed ID: 3223947

DOI: 10.1042/bj2560703

PubMed ID: 2594752

Title: Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1).

PubMed ID: 2594752

DOI: 10.1073/pnas.86.23.9089

PubMed ID: 16252102

Title: Recessive distal renal tubular acidosis in Sarawak caused by AE1 mutations.

PubMed ID: 16252102

DOI: 10.1007/s00467-005-2061-z

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 2790053

Title: Primary structure of the cytoplasmic domain of human erythrocyte protein band 3. Comparison with its sequence in the mouse.

PubMed ID: 2790053

DOI: 10.1016/0167-4838(89)90116-7

PubMed ID: 6345535

Title: Amino acid sequence of the N alpha-terminal 201 residues of human erythrocyte membrane band 3.

PubMed ID: 6345535

DOI: 10.1016/s0021-9258(20)82016-x

PubMed ID: 701248

Title: Orientation of the band 3 polypeptide from human erythrocyte membranes. Identification of NH2-terminal sequence and site of carbohydrate attachment.

PubMed ID: 701248

DOI: 10.1016/s0021-9258(17)34491-5

PubMed ID: 7506871

Title: Anion exchanger 1 in human kidney and oncocytoma differs from erythroid AE1 in its NH2 terminus.

PubMed ID: 7506871

DOI: 10.1152/ajprenal.1993.265.6.f813

PubMed ID: 1527044

Title: A structural study of the membrane domain of band 3 by tryptic digestion. Conformational change of band 3 in situ induced by alkali treatment.

PubMed ID: 1527044

DOI: 10.1016/s0021-9258(18)41763-2

PubMed ID: 6615451

Title: The human erythrocyte anion-transport protein. Partial amino acid sequence, conformation and a possible molecular mechanism for anion exchange.

PubMed ID: 6615451

DOI: 10.1042/bj2130577

PubMed ID: 1352774

Title: Anion-proton cotransport through the human red blood cell band 3 protein. Role of glutamate 681.

PubMed ID: 1352774

DOI: 10.1016/s0021-9258(19)49664-6

PubMed ID: 8547122

Title: Band 3 Chur: a variant associated with band 3-deficient hereditary spherocytosis and substitution in a highly conserved position of transmembrane segment 11.

PubMed ID: 8547122

DOI: 10.1111/j.1365-2141.1995.tb05393.x

PubMed ID: 3372523

Title: Localization of the pyridoxal phosphate binding site at the COOH-terminal region of erythrocyte band 3 protein.

PubMed ID: 3372523

DOI: 10.1016/s0021-9258(18)68468-6

PubMed ID: 2204832

Title: Expression, purification, biochemical characterization and inhibition of recombinant Plasmodium falciparum aldolase.

PubMed ID: 2204832

DOI: 10.1016/0166-6851(90)90189-s

PubMed ID: 1998697

Title: Phosphorylation sites in human erythrocyte band 3 protein.

PubMed ID: 1998697

DOI: 10.1016/0005-2736(91)90291-f

PubMed ID: 1885574

Title: Palmitoylation of cysteine 69 from the COOH-terminal of band 3 protein in the human erythrocyte membrane. Acylation occurs in the middle of the consensus sequence of F--I-IICLAVL found in band 3 protein and G2 protein of Rift Valley fever virus.

PubMed ID: 1885574

DOI: 10.1016/s0021-9258(18)55315-1

PubMed ID: 7665627

Title: The ANK repeats of erythrocyte ankyrin form two distinct but cooperative binding sites for the erythrocyte anion exchanger.

PubMed ID: 7665627

DOI: 10.1074/jbc.270.37.22050

PubMed ID: 10861210

Title: Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein.

PubMed ID: 10861210

DOI: 10.1042/0264-6021:3490051

PubMed ID: 10942405

Title: Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine kinases in intact human erythrocytes: identification of primary and secondary phosphorylation sites.

PubMed ID: 10942405

PubMed ID: 12692305

Title: Band 3 is a host receptor binding merozoite surface protein 1 during the Plasmodium falciparum invasion of erythrocytes.

PubMed ID: 12692305

DOI: 10.1073/pnas.0834959100

PubMed ID: 14630931

Title: A co-ligand complex anchors Plasmodium falciparum merozoites to the erythrocyte invasion receptor band 3.

PubMed ID: 14630931

DOI: 10.1074/jbc.m308716200

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 23219802

Title: Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains.

PubMed ID: 23219802

DOI: 10.1016/j.bbamem.2012.11.030

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 26049106

Title: Transmembrane protein 139 (TMEM139) interacts with human kidney isoform of anion exchanger 1 (kAE1).

PubMed ID: 26049106

DOI: 10.1016/j.bbrc.2015.05.128

PubMed ID: 28387307

Title: Stomatin modulates the activity of the Anion Exchanger 1 (AE1, SLC4A1).

PubMed ID: 28387307

DOI: 10.1038/srep46170

PubMed ID: 8508760

Title: Two-dimensional structure of the membrane domain of human band 3, the anion transport protein of the erythrocyte membrane.

PubMed ID: 8508760

DOI: 10.1002/j.1460-2075.1993.tb05876.x

PubMed ID: 8045253

Title: Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3.

PubMed ID: 8045253

DOI: 10.1002/j.1460-2075.1994.tb06624.x

PubMed ID: 8168533

Title: The solution structures of the first and second transmembrane-spanning segments of band 3.

PubMed ID: 8168533

DOI: 10.1111/j.1432-1033.1994.tb18757.x

PubMed ID: 8527430

Title: Solution structure of a band 3 peptide inhibitor bound to aldolase: a proposed mechanism for regulating binding by tyrosine phosphorylation.

PubMed ID: 8527430

DOI: 10.1021/bi00051a005

PubMed ID: 9454576

Title: Insights into tyrosine phosphorylation control of protein-protein association from the NMR structure of a band 3 peptide inhibitor bound to glyceraldehyde-3-phosphate dehydrogenase.

PubMed ID: 9454576

DOI: 10.1021/bi971445b

PubMed ID: 9765907

Title: Studies on the structure of a transmembrane region and a cytoplasmic loop of the human red cell anion exchanger.

PubMed ID: 9765907

DOI: 10.1042/bst0260516

PubMed ID: 9709005

Title: NMR solution structure of a cytoplasmic surface loop of the human red cell anion transporter, band 3.

PubMed ID: 9709005

DOI: 10.1021/bi973158d

PubMed ID: 11049968

Title: Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3.

PubMed ID: 11049968

PubMed ID: 24121512

Title: A substrate access tunnel in the cytosolic domain is not an essential feature of the solute carrier 4 (SLC4) family of bicarbonate transporters.

PubMed ID: 24121512

DOI: 10.1074/jbc.m113.511865

PubMed ID: 26542571

Title: Crystal structure of the anion exchanger domain of human erythrocyte band 3.

PubMed ID: 26542571

DOI: 10.1126/science.aaa4335

PubMed ID: 35835865

Title: Architecture of the human erythrocyte ankyrin-1 complex.

PubMed ID: 35835865

DOI: 10.1038/s41594-022-00792-w

PubMed ID: 1678289

Title: Human erythrocyte band 3 polymorphism (band 3 Memphis): characterization of the structural modification (Lys 56-->Glu) by protein chemistry methods.

PubMed ID: 1678289

PubMed ID: 1722314

Title: Deletion in erythrocyte band 3 gene in malaria-resistant Southeast Asian ovalocytosis.

PubMed ID: 1722314

DOI: 10.1073/pnas.88.24.11022

PubMed ID: 1378323

Title: Band 3 Tuscaloosa: Pro-327-->Arg substitution in the cytoplasmic domain of erythrocyte band 3 protein associated with spherocytic hemolytic anemia and partial deficiency of protein 4.2.

PubMed ID: 1378323

PubMed ID: 1538405

Title: Basis of unique red cell membrane properties in hereditary ovalocytosis.

PubMed ID: 1538405

DOI: 10.1016/0022-2836(92)90254-h

PubMed ID: 8343110

Title: Band 3 HT, a human red-cell variant associated with acanthocytosis and increased anion transport, carries the mutation Pro-868-->Leu in the membrane domain of band 3.

PubMed ID: 8343110

DOI: 10.1042/bj2930317

PubMed ID: 8471774

Title: Human erythrocyte protein 4.2 deficiency associated with hemolytic anemia and a homozygous 40 glutamic acid-->lysine substitution in the cytoplasmic domain of band 3 (band 3Montefiore).

PubMed ID: 8471774

PubMed ID: 8206915

Title: Band 3 Memphis variant II. Altered stilbene disulfonate binding and the Diego (Dia) blood group antigen are associated with the human erythrocyte band 3 mutation Pro-854-->Leu.

PubMed ID: 8206915

DOI: 10.1016/s0021-9258(17)33986-8

PubMed ID: 7812009

Title: Changes in the blood group Wright antigens are associated with a mutation at amino acid 658 in human erythrocyte band 3: a site of interaction between band 3 and glycophorin A under certain conditions.

PubMed ID: 7812009

PubMed ID: 7530501

Title: Mutations of conserved arginines in the membrane domain of erythroid band 3 lead to a decrease in membrane-associated band 3 and to the phenotype of hereditary spherocytosis.

PubMed ID: 7530501

PubMed ID: 8943874

Title: Characterization of 13 novel band 3 gene defects in hereditary spherocytosis with band 3 deficiency.

PubMed ID: 8943874

PubMed ID: 8640229

Title: Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis.

PubMed ID: 8640229

DOI: 10.1038/ng0696-214

PubMed ID: 9207478

Title: Modulation of clinical expression and band 3 deficiency in hereditary spherocytosis.

PubMed ID: 9207478

PubMed ID: 9012689

Title: Novel band 3 variants (bands 3 Foggia, Napoli I and Napoli II) associated with hereditary spherocytosis and band 3 deficiency: status of the D38A polymorphism within the EPB3 locus.

PubMed ID: 9012689

DOI: 10.1046/j.1365-2141.1997.8732504.x

PubMed ID: 9233560

Title: Heterogenous band 3 deficiency in hereditary spherocytosis related to different band 3 gene defects.

PubMed ID: 9233560

DOI: 10.1046/j.1365-2141.1997.1893005.x

PubMed ID: 9312167

Title: Familial distal renal tubular acidosis is associated with mutations in the red cell anion exchanger (Band 3, AE1) gene.

PubMed ID: 9312167

DOI: 10.1172/jci119694

PubMed ID: 9191821

Title: Blood group antigens Rb(a), Tr(a), and Wd(a) are located in the third ectoplasmic loop of erythroid band 3.

PubMed ID: 9191821

DOI: 10.1046/j.1537-2995.1997.37697335155.x

PubMed ID: 9973643

Title: Band 3 Tokyo: Thr837-->Ala837 substitution in erythrocyte band 3 protein associated with spherocytic hemolysis.

PubMed ID: 9973643

DOI: 10.1159/000040904

PubMed ID: 9845551

Title: Characterization of seven low incidence blood group antigens carried by erythrocyte band 3 protein.

PubMed ID: 9845551

PubMed ID: 9854053

Title: Novel AE1 mutations in recessive distal renal tubular acidosis: loss-of-function is rescued by glycophorin A.

PubMed ID: 9854053

DOI: 10.1172/jci4836

PubMed ID: 9600966

Title: Mutations in the chloride-bicarbonate exchanger gene AE1 cause autosomal dominant but not autosomal recessive distal renal tubular acidosis.

PubMed ID: 9600966

DOI: 10.1073/pnas.95.11.6337

PubMed ID: 9709782

Title: A Gly565-->Ala substitution in human erythroid band 3 accounts for the Wu blood group polymorphism.

PubMed ID: 9709782

DOI: 10.1046/j.1537-2995.1998.38898375513.x

PubMed ID: 10580570

Title: Arginine 490 is a hot spot for mutation in the band 3 gene in hereditary spherocytosis.

PubMed ID: 10580570

DOI: 10.1111/j.1600-0609.1999.tb01141.x

PubMed ID: 10926824

Title: Band 3 mutations, renal tubular acidosis and South-East Asian ovalocytosis in Malaysia and Papua New Guinea: loss of up to 95% band 3 transport in red cells.

PubMed ID: 10926824

DOI: 10.1042/bj3500041

PubMed ID: 10942416

Title: Severe hereditary spherocytosis and distal renal tubular acidosis associated with the total absence of band 3.

PubMed ID: 10942416

PubMed ID: 10745622

Title: Characteristic features of the genotype and phenotype of hereditary spherocytosis in the Japanese population.

PubMed ID: 10745622

PubMed ID: 11208088

Title: Trafficking and folding defects in hereditary spherocytosis mutants of the human red cell anion exchanger.

PubMed ID: 11208088

DOI: 10.1034/j.1600-0854.2000.011208.x

PubMed ID: 10738034

Title: Amino acid substitutions in human erythroid protein band 3 account for the low-incidence antigens NFLD and BOW.

PubMed ID: 10738034

DOI: 10.1046/j.1537-2995.2000.40030325.x

PubMed ID: 11061863

Title: An amino acid substitution in the putative second extracellular loop of RBC band 3 accounts for the Froese blood group polymorphism.

PubMed ID: 11061863

DOI: 10.1046/j.1537-2995.2000.40101246.x

PubMed ID: 11155072

Title: Distinctive Swann blood group genotypes: molecular investigations.

PubMed ID: 11155072

DOI: 10.1159/000056733

PubMed ID: 11380459

Title: Band 3 Cape Town (E90K) causes severe hereditary spherocytosis in combination with band 3 Prague III.

PubMed ID: 11380459

DOI: 10.1046/j.1365-2141.2001.02800.x

PubMed ID: 15211439

Title: Novel compound heterozygous SLC4A1 mutations in Thai patients with autosomal recessive distal renal tubular acidosis.

PubMed ID: 15211439

DOI: 10.1053/j.ajkd.2004.03.033

PubMed ID: 14734552

Title: A novel missense mutation in AE1 causing autosomal dominant distal renal tubular acidosis retains normal transport function but is mistargeted in polarized epithelial cells.

PubMed ID: 14734552

DOI: 10.1074/jbc.m400188200

PubMed ID: 15813913

Title: Band 3Tambau: a de novo mutation in the AE1 gene associated with hereditary spherocytosis. Implications for anion exchange and insertion into the red blood cell membrane.

PubMed ID: 15813913

DOI: 10.1111/j.1600-0609.2004.00405.x

PubMed ID: 16227998

Title: Monovalent cation leaks in human red cells caused by single amino-acid substitutions in the transport domain of the band 3 chloride-bicarbonate exchanger, AE1.

PubMed ID: 16227998

DOI: 10.1038/ng1656

PubMed ID: 20151848

Title: Impaired trafficking and intracellular retention of mutant kidney anion exchanger 1 proteins (G701D and A858D) associated with distal renal tubular acidosis.

PubMed ID: 20151848

DOI: 10.3109/09687681003588020

PubMed ID: 21849667

Title: Loss-of-function and gain-of-function phenotypes of stomatocytosis mutant RhAG F65S.

PubMed ID: 21849667

DOI: 10.1152/ajpcell.00054.2011

PubMed ID: 36320073

Title: Impaired trafficking and instability of mutant kidney anion exchanger 1 proteins associated with autosomal recessive distal renal tubular acidosis.

PubMed ID: 36320073

DOI: 10.1186/s12920-022-01381-y

Sequence Information:

  • Length: 911
  • Mass: 101792
  • Checksum: 35EC3EE7AFF27D2F
  • Sequence:
    • MEELQDDYED MMEENLEQEE YEDPDIPESQ MEEPAAHDTE ATATDYHTTS HPGTHKVYVE 
LQELVMDEKN QELRWMEAAR WVQLEENLGE NGAWGRPHLS HLTFWSLLEL RRVFTKGTVL 
LDLQETSLAG VANQLLDRFI FEDQIRPQDR EELLRALLLK HSHAGELEAL GGVKPAVLTR 
SGDPSQPLLP QHSSLETQLF CEQGDGGTEG HSPSGILEKI PPDSEATLVL VGRADFLEQP 
VLGFVRLQEA AELEAVELPV PIRFLFVLLG PEAPHIDYTQ LGRAAATLMS ERVFRIDAYM 
AQSRGELLHS LEGFLDCSLV LPPTDAPSEQ ALLSLVPVQR ELLRRRYQSS PAKPDSSFYK 
GLDLNGGPDD PLQQTGQLFG GLVRDIRRRY PYYLSDITDA FSPQVLAAVI FIYFAALSPA 
ITFGGLLGEK TRNQMGVSEL LISTAVQGIL FALLGAQPLL VVGFSGPLLV FEEAFFSFCE 
TNGLEYIVGR VWIGFWLILL VVLVVAFEGS FLVRFISRYT QEIFSFLISL IFIYETFSKL 
IKIFQDHPLQ KTYNYNVLMV PKPQGPLPNT ALLSLVLMAG TFFFAMMLRK FKNSSYFPGK 
LRRVIGDFGV PISILIMVLV DFFIQDTYTQ KLSVPDGFKV SNSSARGWVI HPLGLRSEFP 
IWMMFASALP ALLVFILIFL ESQITTLIVS KPERKMVKGS GFHLDLLLVV GMGGVAALFG 
MPWLSATTVR SVTHANALTV MGKASTPGAA AQIQEVKEQR ISGLLVAVLV GLSILMEPIL 
SRIPLAVLFG IFLYMGVTSL SGIQLFDRIL LLFKPPKYHP DVPYVKRVKT WRMHLFTGIQ 
IICLAVLWVV KSTPASLALP FVLILTVPLR RVLLPLIFRN VELQCLDADD AKATFDEEEG 
RDEYDEVAMP V

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.