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Protein

Band 3 anion transport protein

Gene

SLC4A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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 exchange in the kidney, and is required for normal acidification of the urine.5 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Phenyl isothiocyanate inhibits anion transport in vitro.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei590Important for anion transport1
Sitei681Important for anion-proton cotransport1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionBlood group antigen
Biological processAnion exchange, Ion transport, Transport

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1237044 Erythrocytes take up carbon dioxide and release oxygen
R-HSA-1247673 Erythrocytes take up oxygen and release carbon dioxide
R-HSA-425381 Bicarbonate transporters
R-HSA-5619050 Defective SLC4A1 causes hereditary spherocytosis type 4 (HSP4), distal renal tubular acidosis (dRTA) and dRTA with hemolytic anemia (dRTA-HA)

SIGNOR Signaling Network Open Resource

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SIGNORi
P02730

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P02730 Curated

MoonProt database of moonlighting proteins

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MoonProti
P02730

Transport Classification Database

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TCDBi
2.A.31.1.1 the anion exchanger (ae) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Band 3 anion transport protein
Alternative name(s):
Anion exchange protein 1
Short name:
AE 1
Short name:
Anion exchanger 1
Solute carrier family 4 member 1
CD_antigen: CD233
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SLC4A1
Synonyms:AE1, DI, EPB3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 17

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000004939.13

Human Gene Nomenclature Database

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HGNCi
HGNC:11027 SLC4A1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
109270 gene+phenotype

neXtProt; the human protein knowledge platform

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neXtProti
NX_P02730

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 403Cytoplasmic1 PublicationAdd BLAST403
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei404 – 427Helical; Name=11 PublicationAdd BLAST24
Topological domaini428 – 435Extracellular1 Publication8
Transmembranei436 – 456Helical; Name=21 PublicationAdd BLAST21
Topological domaini457 – 459Cytoplasmic1 Publication3
Transmembranei460 – 476Discontinuously helical; Name=31 PublicationAdd BLAST17
Topological domaini477 – 485Extracellular1 Publication9
Transmembranei486 – 506Helical; Name=41 PublicationAdd BLAST21
Topological domaini507 – 518Cytoplasmic1 PublicationAdd BLAST12
Transmembranei519 – 541Helical; Name=51 PublicationAdd BLAST23
Topological domaini542 – 570Extracellular1 PublicationAdd BLAST29
Transmembranei571 – 591Helical; Name=61 PublicationAdd BLAST21
Topological domaini592 – 602Cytoplasmic1 PublicationAdd BLAST11
Transmembranei603 – 623Helical; Name=71 PublicationAdd BLAST21
Topological domaini624 – 663Extracellular1 PublicationAdd BLAST40
Transmembranei664 – 684Helical; Name=81 PublicationAdd BLAST21
Topological domaini685 – 700Cytoplasmic1 PublicationAdd BLAST16
Transmembranei701 – 719Helical; Name=91 PublicationAdd BLAST19
Transmembranei720 – 737Discontinuously helical; Name=101 PublicationAdd BLAST18
Topological domaini738 – 760Cytoplasmic1 PublicationAdd BLAST23
Transmembranei761 – 781Helical; Name=111 PublicationAdd BLAST21
Transmembranei782 – 800Helical; Name=121 PublicationAdd BLAST19
Topological domaini801 – 838Cytoplasmic1 PublicationAdd BLAST38
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei839 – 869Discontinuously helical1 PublicationAdd BLAST31
Topological domaini870 – 911Cytoplasmic1 PublicationAdd BLAST42

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Ovalocytosis, Southeast Asian (SAO)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA hereditary hematologic disorder characterized by ovalocytic erythrocytes that are rigid and exhibit reduced expression of many erythrocyte antigens. Clinical manifestations include mild hemolysis, intermittent jaundice and gallstones. However, the disorder is most often asymptomatic.
See also OMIM:166900
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000801400 – 408Missing in SAO; increased rigidity of the erythrocyte membrane leading to increased resistance to shear stress and increased resistance to P.falciparum. 2 Publications9
Spherocytosis 4 (SPH4)15 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionSpherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal.
See also OMIM:612653
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01378490E → K in SPH4; Cape Town. 1 PublicationCorresponds to variant dbSNP:rs28929480EnsemblClinVar.1
Natural variantiVAR_013785130G → R in SPH4; Fukoka. 1 PublicationCorresponds to variant dbSNP:rs121912749EnsemblClinVar.1
Natural variantiVAR_013786147P → S in SPH4; Mondego. 1 Publication1
Natural variantiVAR_013787285A → D in SPH4; Boston. 1 Publication1
Natural variantiVAR_000800327P → R in SPH4; Tuscaloosa. 1 PublicationCorresponds to variant dbSNP:rs28931583EnsemblClinVar.1
Natural variantiVAR_013789455G → E in SPH4; Benesov. 1 Publication1
Natural variantiVAR_058038455G → R in SPH4; Yamagata. 1 Publication1
Natural variantiVAR_013791488V → M in SPH4; Coimbra; also in AR-dRTA. 2 PublicationsCorresponds to variant dbSNP:rs28931584EnsemblClinVar.1
Natural variantiVAR_013792490R → C in SPH4; Bicetre I. 1 PublicationCorresponds to variant dbSNP:rs1398477044Ensembl.1
Natural variantiVAR_058039490R → H in SPH4; Pinhal. 1 Publication1
Natural variantiVAR_000802518R → C in SPH4; Dresden. 1 PublicationCorresponds to variant dbSNP:rs868742796Ensembl.1
Natural variantiVAR_058042663M → K in SPH4; Tambau. 1 Publication1
Natural variantiVAR_000807663Missing in SPH4; Osnabruck II. 1 Publication1
Natural variantiVAR_039294705D → Y in SPH4; Horam; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport. 1 Publication1
Natural variantiVAR_013804707L → P in SPH4; Most. 2 Publications1
Natural variantiVAR_013805714G → R in SPH4; Okinawa. 1 Publication1
Natural variantiVAR_013806760R → Q in SPH4; Prague II; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport. 4 PublicationsCorresponds to variant dbSNP:rs121912755EnsemblClinVar.1
Natural variantiVAR_013807760R → W in SPH4; Hradec Kralove. 3 PublicationsCorresponds to variant dbSNP:rs373916826Ensembl.1
Natural variantiVAR_013808771G → D in SPH4; Chur. 1 PublicationCorresponds to variant dbSNP:rs121912741EnsemblClinVar.1
Natural variantiVAR_013809783I → N in SPH4; Napoli II. 1 Publication1
Natural variantiVAR_013810808R → C in SPH4; Jablonec. 2 PublicationsCorresponds to variant dbSNP:rs1167814744Ensembl.1
Natural variantiVAR_013811808R → H in SPH4; Nara. 1 PublicationCorresponds to variant dbSNP:rs866727908EnsemblClinVar.1
Natural variantiVAR_013812834H → P in SPH4; Birmingham. 2 Publications1
Natural variantiVAR_013813837T → A in SPH4; Tokyo. 1 PublicationCorresponds to variant dbSNP:rs121912750EnsemblClinVar.1
Natural variantiVAR_013814837T → M in SPH4; Philadelphia. 4 Publications1
Natural variantiVAR_058043837T → R in SPH4; Nagoya. 1 Publication1
Natural variantiVAR_013816870R → W in SPH4; Prague III. 3 PublicationsCorresponds to variant dbSNP:rs28931585EnsemblClinVar.1
Renal tubular acidosis, distal, autosomal dominant (AD-dRTA)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disease characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis. It is due to functional failure of alpha-intercalated cells of the cortical collecting duct of the distal nephron, where vectorial proton transport is required for urinary acidification.
See also OMIM:179800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015104589R → C in AD-dRTA; reduced red cell sulfate transport and altered glycosylation of the red cell band 3 N-glycan chain. 1 PublicationCorresponds to variant dbSNP:rs121912745EnsemblClinVar.1
Natural variantiVAR_015105589R → H in AD-dRTA. 2 PublicationsCorresponds to variant dbSNP:rs121912744EnsemblClinVar.1
Natural variantiVAR_015106589R → S in AD-dRTA. 1 PublicationCorresponds to variant dbSNP:rs121912745EnsemblClinVar.1
Natural variantiVAR_058041609G → R in AD-dRTA; detected subapically and at the apical membrane as well as at the basolateral membrane in contrast to the normal basolateral appearance of wild-type protein. 1 PublicationCorresponds to variant dbSNP:rs878853002EnsemblClinVar.1
Natural variantiVAR_015107613S → F in AD-dRTA; markedly increased red cell sulfate transport but almost normal red cell iodide transport. 1 PublicationCorresponds to variant dbSNP:rs121912746EnsemblClinVar.1
Natural variantiVAR_015108858A → D in AD-dRTA; impairs expression at the cell membrane. 2 PublicationsCorresponds to variant dbSNP:rs121912751EnsemblClinVar.1
Renal tubular acidosis, distal, with hemolytic anemia (dRTA-HA)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by the association of hemolytic anemia with distal renal tubular acidosis, the reduced ability to acidify urine resulting in variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis.
See also OMIM:611590
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_039292602R → P in dRTA-HA. 1 PublicationCorresponds to variant dbSNP:rs121912754EnsemblClinVar.1
Natural variantiVAR_015171701G → D in dRTA-HA; impairs expression at the cell membrane. 3 PublicationsCorresponds to variant dbSNP:rs121912748EnsemblClinVar.1
Natural variantiVAR_015109850Missing in dRTA-HA. 1 Publication1
Renal tubular acidosis, distal, with normal red cell morphology (dRTA-NRC)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis. It is due to functional failure of alpha-intercalated cells of the cortical collecting duct of the distal nephron, where vectorial proton transport is required for urinary acidification.
See also OMIM:611590
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_039297773S → P in dRTA-NRC. 1 PublicationCorresponds to variant dbSNP:rs121912753EnsemblClinVar.1
Cryohydrocytosis (CHC)1 Publication
The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder of red cell membrane permeability characterized by cold-induced changes in cell volume, resulting in cold-sensitive stomatocytosis, and increased erythrocyte osmotic fragility and autohemolysis at 4 degrees Celsius. Patients present with mild to moderate hemolytic anemia, splenomegaly, fatigue, and pseudohyperkalemia due to a potassium leak from the erythrocytes.
See also OMIM:185020
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_039293687L → P in CHC; Blackburn; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport. 1 PublicationCorresponds to variant dbSNP:rs863225463EnsemblClinVar.1
Natural variantiVAR_039295731S → P in CHC; Hemel; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport. 1 PublicationCorresponds to variant dbSNP:rs863225461EnsemblClinVar.1
Natural variantiVAR_039296734H → R in CHC; Hurstpierpont; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport. 1 PublicationCorresponds to variant dbSNP:rs863225462EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi85E → A or R: Impairs expression at the cell membrane. 1 Publication1
Mutagenesisi283R → A, E or S: Impairs expression at the cell membrane. 1 Publication1
Mutagenesisi642N → D: Loss of N-glycosylation site. 1 Publication1
Mutagenesisi681E → Q: Impairs expression at the cell membrane. 1 Publication1

Keywords - Diseasei

Disease mutation, Elliptocytosis, Hereditary hemolytic anemia

Organism-specific databases

DisGeNET

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DisGeNETi
6521

MalaCards human disease database

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MalaCardsi
SLC4A1
MIMi109270 gene+phenotype
110500 phenotype
112010 phenotype
112050 phenotype
130600 phenotype
166900 phenotype
179800 phenotype
185020 phenotype
601550 phenotype
601551 phenotype
611162 phenotype
611590 phenotype
612653 phenotype

Open Targets

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OpenTargetsi
ENSG00000004939

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
93608 Autosomal dominant distal renal tubular acidosis
3202 Dehydrated hereditary stomatocytosis
93610 Distal renal tubular acidosis with anemia
398088 Hereditary cryohydrocytosis with normal stomatin
822 Hereditary spherocytosis
98868 Southeast Asian ovalocytosis

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA35895

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
SLC4A1

Domain mapping of disease mutations (DMDM)

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DMDMi
114787

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000792091 – 911Band 3 anion transport proteinAdd BLAST911

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionine2 Publications1
Modified residuei8Phosphotyrosine2 Publications1
Modified residuei21Phosphotyrosine2 Publications1
Modified residuei46Phosphotyrosine1 Publication1
Modified residuei185PhosphoserineBy similarity1
Modified residuei350PhosphoserineBy similarity1
Modified residuei359Phosphotyrosine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi642N-linked (GlcNAc...) (complex) asparagine2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi843S-palmitoyl cysteine1 Publication1
Modified residuei904Phosphotyrosine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated on Tyr-8 and Tyr-21 most likely by SYK. PP1-resistant phosphorylation that precedes Tyr-359 and Tyr-904 phosphorylation.2 Publications
Phosphorylated on Tyr-359 and Tyr-904 most likely by LYN. PP1-inhibited phosphorylation that follows Tyr-8 and Tyr-21 phosphorylation.2 Publications
N-glycosylated.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P02730

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P02730

PeptideAtlas

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PeptideAtlasi
P02730

PRoteomics IDEntifications database

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PRIDEi
P02730

ProteomicsDB human proteome resource

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ProteomicsDBi
51557

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
1024

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P02730

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P02730

SwissPalm database of S-palmitoylation events

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SwissPalmi
P02730

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P02730

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in erythrocytes (at protein level) (PubMed:7506871, PubMed:26542571). Isoform 2 is expressed in kidney (at protein level) (PubMed:7506871).5 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000004939 Expressed in 131 organ(s), highest expression level in trabecular bone tissue

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P02730 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P02730 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB034438
HPA015584
HPA063911

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

A dimer in solution, but in its membrane environment, it exists primarily as a mixture of dimers and tetramers and spans the membrane asymmetrically. Interacts (via cytoplasmic N-terminal domain) with ANK1 (via N-terminal ANK repeats); tetramer formation is critical for ankyrin association. Interacts with STOM. Isoform 2 interacts with TM139 (PubMed:26049106).5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
112412, 12 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P02730

Database of interacting proteins

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DIPi
DIP-42428N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P02730

Protein interaction database and analysis system

More...
IntActi
P02730, 25 interactors

Molecular INTeraction database

More...
MINTi
P02730

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000262418

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1911
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BH7NMR-A803-835[»]
1BNXNMR-A389-430[»]
1BTQNMR-A405-424[»]
1BTRNMR-A405-424[»]
1BTSNMR-A436-456[»]
1BTTNMR-A436-456[»]
1BZKNMR-A389-430[»]
1HYNX-ray2.60P/Q/R/S1-379[»]
2BTANMR-A1-15[»]
2BTBNMR-A1-15[»]
3BTBNMR-A1-15[»]
4KY9X-ray2.23A/P51-356[»]
4YZFX-ray3.50A/B/C/D1-911[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P02730

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P02730

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P02730

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni55 – 290GlobularAdd BLAST236
Regioni176 – 185Interaction with ANK1Curated10
Regioni304 – 357Dimerization armAdd BLAST54
Regioni559 – 630Involved in anion transportAdd BLAST72

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1172 Eukaryota
ENOG410XPHD LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157423

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG004326

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P02730

KEGG Orthology (KO)

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KOi
K06573

Identification of Orthologs from Complete Genome Data

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OMAi
FIYEEQI

Database of Orthologous Groups

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OrthoDBi
265068at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P02730

TreeFam database of animal gene trees

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TreeFami
TF313630

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.930.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001717 Anion_exchange
IPR002977 Anion_exchange_1
IPR018241 Anion_exchange_CS
IPR013769 Band3_cytoplasmic_dom
IPR011531 HCO3_transpt_C
IPR003020 HCO3_transpt_euk
IPR016152 PTrfase/Anion_transptr

The PANTHER Classification System

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PANTHERi
PTHR11453 PTHR11453, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF07565 Band_3_cyto, 1 hit
PF00955 HCO3_cotransp, 2 hits

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00165 ANIONEXCHNGR
PR01187 ANIONEXHNGR1
PR01231 HCO3TRNSPORT

Superfamily database of structural and functional annotation

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SUPFAMi
SSF55804 SSF55804, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00834 ae, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00219 ANION_EXCHANGER_1, 1 hit
PS00220 ANION_EXCHANGER_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P02730-1) [UniParc]FASTAAdd to basket
Also known as: eAE1, Erythrocyte

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MEELQDDYED MMEENLEQEE YEDPDIPESQ MEEPAAHDTE ATATDYHTTS
60 70 80 90 100
HPGTHKVYVE LQELVMDEKN QELRWMEAAR WVQLEENLGE NGAWGRPHLS
110 120 130 140 150
HLTFWSLLEL RRVFTKGTVL LDLQETSLAG VANQLLDRFI FEDQIRPQDR
160 170 180 190 200
EELLRALLLK HSHAGELEAL GGVKPAVLTR SGDPSQPLLP QHSSLETQLF
210 220 230 240 250
CEQGDGGTEG HSPSGILEKI PPDSEATLVL VGRADFLEQP VLGFVRLQEA
260 270 280 290 300
AELEAVELPV PIRFLFVLLG PEAPHIDYTQ LGRAAATLMS ERVFRIDAYM
310 320 330 340 350
AQSRGELLHS LEGFLDCSLV LPPTDAPSEQ ALLSLVPVQR ELLRRRYQSS
360 370 380 390 400
PAKPDSSFYK GLDLNGGPDD PLQQTGQLFG GLVRDIRRRY PYYLSDITDA
410 420 430 440 450
FSPQVLAAVI FIYFAALSPA ITFGGLLGEK TRNQMGVSEL LISTAVQGIL
460 470 480 490 500
FALLGAQPLL VVGFSGPLLV FEEAFFSFCE TNGLEYIVGR VWIGFWLILL
510 520 530 540 550
VVLVVAFEGS FLVRFISRYT QEIFSFLISL IFIYETFSKL IKIFQDHPLQ
560 570 580 590 600
KTYNYNVLMV PKPQGPLPNT ALLSLVLMAG TFFFAMMLRK FKNSSYFPGK
610 620 630 640 650
LRRVIGDFGV PISILIMVLV DFFIQDTYTQ KLSVPDGFKV SNSSARGWVI
660 670 680 690 700
HPLGLRSEFP IWMMFASALP ALLVFILIFL ESQITTLIVS KPERKMVKGS
710 720 730 740 750
GFHLDLLLVV GMGGVAALFG MPWLSATTVR SVTHANALTV MGKASTPGAA
760 770 780 790 800
AQIQEVKEQR ISGLLVAVLV GLSILMEPIL SRIPLAVLFG IFLYMGVTSL
810 820 830 840 850
SGIQLFDRIL LLFKPPKYHP DVPYVKRVKT WRMHLFTGIQ IICLAVLWVV
860 870 880 890 900
KSTPASLALP FVLILTVPLR RVLLPLIFRN VELQCLDADD AKATFDEEEG
910
RDEYDEVAMP V
Length:911
Mass (Da):101,792
Last modified:April 1, 1990 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i35EC3EE7AFF27D2F
GO
Isoform 21 Publication (identifier: P02730-2) [UniParc]FASTAAdd to basket
Also known as: kAE1, Kidney

The sequence of this isoform differs from the canonical sequence as follows:
     1-65: Missing.

Show »
Length:846
Mass (Da):94,195
Checksum:i4008B53D0121A617
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0A0MS98A0A0A0MS98_HUMAN
Band 3 anion transport protein
SLC4A1
545Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
V9H0V9V9H0V9_HUMAN
Anion exchanger
SLC4A1
36Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti11M → D AA sequence (PubMed:6345535).Curated1
Sequence conflicti68E → EE AA sequence (PubMed:6345535).Curated1
Sequence conflicti759Q → H in ABD74692 (PubMed:16252102).Curated1

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

SLC4A1 is responsible for the Diego blood group system [MIMi:110500]. The molecular basis of the Di(a)=Di1/Di(b)/Di2 blood group antigens is a single variation in position 854; Leu-854 corresponds to Di(a) and Pro-854 to Di(b). The molecular basis of the Wr(a)=Di3/Wr(b)/Di4 blood group antigens is a single variation in position 658; Lys-658 corresponds to Wr(a) and Glu-658 to Wr(b). The blood group antigens Wd(a)=Di5 (Waldner-type) has Met-557; Rb(a)=Di6 has Leu-548 and WARR=Di7 has Ile-552.
SLC4A1 is responsible for the Swann blood group system (SW) [MIMi:601550]. Sw(a+) has a Gln or a Trp at position 646 and Sw(a-) has an Arg.
SLC4A1 is responsible for the Froese blood group system (FR) [MIMi:601551]. FR(a+) has a Lys at position 480 and FR(a-) has a Glu.
Genetic variations in SLC4A1 are involved in resistance to malaria [MIMi:611162].

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05803527P → H1 Publication1
Natural variantiVAR_01461238D → A4 PublicationsCorresponds to variant dbSNP:rs5035EnsemblClinVar.1
Natural variantiVAR_00079840E → K Found in patients with hemolytic anemia; unknown pathological significance; Montefiore. 2 PublicationsCorresponds to variant dbSNP:rs45562031EnsemblClinVar.1
Natural variantiVAR_03669345D → E. Corresponds to variant dbSNP:rs34700496Ensembl.1
Natural variantiVAR_00079956K → E in Di(a)/Memphis-II antigen. 6 PublicationsCorresponds to variant dbSNP:rs5036EnsemblClinVar.1
Natural variantiVAR_03929068E → K. Corresponds to variant dbSNP:rs13306787EnsemblClinVar.1
Natural variantiVAR_05803672E → D1 PublicationCorresponds to variant dbSNP:rs13306788EnsemblClinVar.1
Natural variantiVAR_03929173L → M1 PublicationCorresponds to variant dbSNP:rs781490287Ensembl.1
Natural variantiVAR_01378490E → K in SPH4; Cape Town. 1 PublicationCorresponds to variant dbSNP:rs28929480EnsemblClinVar.1
Natural variantiVAR_014613112R → S. Corresponds to variant dbSNP:rs5037Ensembl.1
Natural variantiVAR_013785130G → R in SPH4; Fukoka. 1 PublicationCorresponds to variant dbSNP:rs121912749EnsemblClinVar.1
Natural variantiVAR_013786147P → S in SPH4; Mondego. 1 Publication1
Natural variantiVAR_013787285A → D in SPH4; Boston. 1 Publication1
Natural variantiVAR_000800327P → R in SPH4; Tuscaloosa. 1 PublicationCorresponds to variant dbSNP:rs28931583EnsemblClinVar.1
Natural variantiVAR_000801400 – 408Missing in SAO; increased rigidity of the erythrocyte membrane leading to increased resistance to shear stress and increased resistance to P.falciparum. 2 Publications9
Natural variantiVAR_058037429E → D in NFLD+ antigen. 1 PublicationCorresponds to variant dbSNP:rs1048804130Ensembl.1
Natural variantiVAR_013788432R → W in ELO antigen. Corresponds to variant dbSNP:rs373768879Ensembl.1
Natural variantiVAR_014614442I → F. Corresponds to variant dbSNP:rs5018Ensembl.1
Natural variantiVAR_013789455G → E in SPH4; Benesov. 1 Publication1
Natural variantiVAR_058038455G → R in SPH4; Yamagata. 1 Publication1
Natural variantiVAR_013790480E → K in FR(a+) antigen. 1 PublicationCorresponds to variant dbSNP:rs121912756EnsemblClinVar.1
Natural variantiVAR_013791488V → M in SPH4; Coimbra; also in AR-dRTA. 2 PublicationsCorresponds to variant dbSNP:rs28931584EnsemblClinVar.1
Natural variantiVAR_013792490R → C in SPH4; Bicetre I. 1 PublicationCorresponds to variant dbSNP:rs1398477044Ensembl.1
Natural variantiVAR_058039490R → H in SPH4; Pinhal. 1 Publication1
Natural variantiVAR_025090508E → K1 PublicationCorresponds to variant dbSNP:rs45568837Ensembl.1
Natural variantiVAR_000802518R → C in SPH4; Dresden. 1 PublicationCorresponds to variant dbSNP:rs868742796Ensembl.1
Natural variantiVAR_000803548P → L in RB(A) antigen. Corresponds to variant dbSNP:rs879202054Ensembl.1
Natural variantiVAR_013793551K → N in TR(A) antigen. 1
Natural variantiVAR_000804552T → I in WARR antigen. 1
Natural variantiVAR_013794555Y → H in VG(a) antigen. 1
Natural variantiVAR_000805557V → M in WD(a) antigen. Corresponds to variant dbSNP:rs121912743EnsemblClinVar.1
Natural variantiVAR_058040561P → A in NFLD+ antigen. 1 Publication1
Natural variantiVAR_013795561P → S in BOW antigen. 1 Publication1
Natural variantiVAR_013796565G → A in WU antigen. Corresponds to variant dbSNP:rs551784583Ensembl.1
Natural variantiVAR_013797566P → A in KREP antigen. 1
Natural variantiVAR_013798566P → S in PN(a) antigen. Corresponds to variant dbSNP:rs1393742050Ensembl.1
Natural variantiVAR_013799569N → K in BP(a) antigen. 1
Natural variantiVAR_014615586M → L. Corresponds to variant dbSNP:rs5019Ensembl.1
Natural variantiVAR_015104589R → C in AD-dRTA; reduced red cell sulfate transport and altered glycosylation of the red cell band 3 N-glycan chain. 1 PublicationCorresponds to variant dbSNP:rs121912745EnsemblClinVar.1
Natural variantiVAR_015105589R → H in AD-dRTA. 2 PublicationsCorresponds to variant dbSNP:rs121912744EnsemblClinVar.1
Natural variantiVAR_015106589R → S in AD-dRTA. 1 PublicationCorresponds to variant dbSNP:rs121912745EnsemblClinVar.1
Natural variantiVAR_039292602R → P in dRTA-HA. 1 PublicationCorresponds to variant dbSNP:rs121912754EnsemblClinVar.1
Natural variantiVAR_058041609G → R in AD-dRTA; detected subapically and at the apical membrane as well as at the basolateral membrane in contrast to the normal basolateral appearance of wild-type protein. 1 PublicationCorresponds to variant dbSNP:rs878853002EnsemblClinVar.1
Natural variantiVAR_015107613S → F in AD-dRTA; markedly increased red cell sulfate transport but almost normal red cell iodide transport. 1 PublicationCorresponds to variant dbSNP:rs121912746EnsemblClinVar.1
Natural variantiVAR_013800646R → Q in SW(a+) antigen. 1 PublicationCorresponds to variant dbSNP:rs121912757EnsemblClinVar.1
Natural variantiVAR_013801646R → W in SW(a+) antigen. 1 PublicationCorresponds to variant dbSNP:rs121912758EnsemblClinVar.1
Natural variantiVAR_013802656R → C in HG(a) antigen. Corresponds to variant dbSNP:rs372514760Ensembl.1
Natural variantiVAR_013803656R → H in MO(a) antigen. Corresponds to variant dbSNP:rs758868427Ensembl.1
Natural variantiVAR_000806658E → K in WR(a) antigen. 1 PublicationCorresponds to variant dbSNP:rs75731670EnsemblClinVar.1
Natural variantiVAR_058042663M → K in SPH4; Tambau. 1 Publication1
Natural variantiVAR_000807663Missing in SPH4; Osnabruck II. 1 Publication1
Natural variantiVAR_039293687L → P in CHC; Blackburn; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport. 1 PublicationCorresponds to variant dbSNP:rs863225463EnsemblClinVar.1
Natural variantiVAR_014616688I → V. Corresponds to variant dbSNP:rs5022Ensembl.1
Natural variantiVAR_014617690S → G. Corresponds to variant dbSNP:rs5023Ensembl.1
Natural variantiVAR_015171701G → D in dRTA-HA; impairs expression at the cell membrane. 3 PublicationsCorresponds to variant dbSNP:rs121912748EnsemblClinVar.1
Natural variantiVAR_039294705D → Y in SPH4; Horam; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport. 1 Publication1
Natural variantiVAR_013804707L → P in SPH4; Most. 2 Publications1
Natural variantiVAR_013805714G → R in SPH4; Okinawa. 1 Publication1
Natural variantiVAR_039295731S → P in CHC; Hemel; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport. 1 PublicationCorresponds to variant dbSNP:rs863225461EnsemblClinVar.1
Natural variantiVAR_039296734H → R in CHC; Hurstpierpont; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport. 1 PublicationCorresponds to variant dbSNP:rs863225462EnsemblClinVar.1
Natural variantiVAR_013806760R → Q in SPH4; Prague II; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport. 4 PublicationsCorresponds to variant dbSNP:rs121912755EnsemblClinVar.1
Natural variantiVAR_013807760R → W in SPH4; Hradec Kralove. 3 PublicationsCorresponds to variant dbSNP:rs373916826Ensembl.1
Natural variantiVAR_013808771G → D in SPH4; Chur. 1 PublicationCorresponds to variant dbSNP:rs121912741EnsemblClinVar.1
Natural variantiVAR_039297773S → P in dRTA-NRC. 1 PublicationCorresponds to variant dbSNP:rs121912753EnsemblClinVar.1
Natural variantiVAR_013809783I → N in SPH4; Napoli II. 1 Publication1
Natural variantiVAR_013810808R → C in SPH4; Jablonec. 2 PublicationsCorresponds to variant dbSNP:rs1167814744Ensembl.1
Natural variantiVAR_013811808R → H in SPH4; Nara. 1 PublicationCorresponds to variant dbSNP:rs866727908EnsemblClinVar.1
Natural variantiVAR_014618832R → H. Corresponds to variant dbSNP:rs5025Ensembl.1
Natural variantiVAR_013812834H → P in SPH4; Birmingham. 2 Publications1
Natural variantiVAR_013813837T → A in SPH4; Tokyo. 1 PublicationCorresponds to variant dbSNP:rs121912750EnsemblClinVar.1
Natural variantiVAR_013814837T → M in SPH4; Philadelphia. 4 Publications1
Natural variantiVAR_058043837T → R in SPH4; Nagoya. 1 Publication1
Natural variantiVAR_015109850Missing in dRTA-HA. 1 Publication1
Natural variantiVAR_000808854P → L in Di(a)/Memphis-II antigen. 2 PublicationsCorresponds to variant dbSNP:rs2285644EnsemblClinVar.1
Natural variantiVAR_015108858A → D in AD-dRTA; impairs expression at the cell membrane. 2 PublicationsCorresponds to variant dbSNP:rs121912751EnsemblClinVar.1
Natural variantiVAR_014619862V → I Polymorphism. 2 PublicationsCorresponds to variant dbSNP:rs5026EnsemblClinVar.1
Natural variantiVAR_013815868P → L in acanthocytosis; slightly increases transporter activity; impairs expression at the cell membrane. 2 PublicationsCorresponds to variant dbSNP:rs121912759EnsemblClinVar.1
Natural variantiVAR_013816870R → W in SPH4; Prague III. 3 PublicationsCorresponds to variant dbSNP:rs28931585EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0578331 – 65Missing in isoform 2. 1 PublicationAdd BLAST65

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X12609 mRNA Translation: CAA31128.1
M27819 mRNA Translation: AAA35514.1
DQ419529 mRNA Translation: ABD74692.1
GQ981383 mRNA Translation: ADN39420.1
GQ981384 mRNA Translation: ADN39421.1
DQ072115 Genomic DNA Translation: AAY57324.1
CH471178 Genomic DNA Translation: EAW51614.1
BC096106 mRNA Translation: AAH96106.1
BC096107 mRNA Translation: AAH96107.1
BC099628 mRNA Translation: AAH99628.1
BC099629 mRNA Translation: AAH99629.1
BC101570 mRNA Translation: AAI01571.1
BC101574 mRNA Translation: AAI01575.1
S68680 mRNA Translation: AAC60608.2

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS11481.1 [P02730-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A36218 B3HU

NCBI Reference Sequences

More...
RefSeqi
NP_000333.1, NM_000342.3 [P02730-1]
XP_005257650.1, XM_005257593.4 [P02730-2]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.210751
Hs.443948

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000262418; ENSP00000262418; ENSG00000004939 [P02730-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
6521

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:6521

UCSC genome browser

More...
UCSCi
uc002igf.5 human [P02730-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Band 3 entry

dbRBC/BGMUT

Blood group antigen gene mutation database

SeattleSNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12609 mRNA Translation: CAA31128.1
M27819 mRNA Translation: AAA35514.1
DQ419529 mRNA Translation: ABD74692.1
GQ981383 mRNA Translation: ADN39420.1
GQ981384 mRNA Translation: ADN39421.1
DQ072115 Genomic DNA Translation: AAY57324.1
CH471178 Genomic DNA Translation: EAW51614.1
BC096106 mRNA Translation: AAH96106.1
BC096107 mRNA Translation: AAH96107.1
BC099628 mRNA Translation: AAH99628.1
BC099629 mRNA Translation: AAH99629.1
BC101570 mRNA Translation: AAI01571.1
BC101574 mRNA Translation: AAI01575.1
S68680 mRNA Translation: AAC60608.2
CCDSiCCDS11481.1 [P02730-1]
PIRiA36218 B3HU
RefSeqiNP_000333.1, NM_000342.3 [P02730-1]
XP_005257650.1, XM_005257593.4 [P02730-2]
UniGeneiHs.210751
Hs.443948

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BH7NMR-A803-835[»]
1BNXNMR-A389-430[»]
1BTQNMR-A405-424[»]
1BTRNMR-A405-424[»]
1BTSNMR-A436-456[»]
1BTTNMR-A436-456[»]
1BZKNMR-A389-430[»]
1HYNX-ray2.60P/Q/R/S1-379[»]
2BTANMR-A1-15[»]
2BTBNMR-A1-15[»]
3BTBNMR-A1-15[»]
4KY9X-ray2.23A/P51-356[»]
4YZFX-ray3.50A/B/C/D1-911[»]
ProteinModelPortaliP02730
SMRiP02730
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112412, 12 interactors
CORUMiP02730
DIPiDIP-42428N
ELMiP02730
IntActiP02730, 25 interactors
MINTiP02730
STRINGi9606.ENSP00000262418

Protein family/group databases

MoonDBiP02730 Curated
MoonProtiP02730
TCDBi2.A.31.1.1 the anion exchanger (ae) family

PTM databases

GlyConnecti1024
iPTMnetiP02730
PhosphoSitePlusiP02730
SwissPalmiP02730

Polymorphism and mutation databases

BioMutaiSLC4A1
DMDMi114787

Proteomic databases

jPOSTiP02730
PaxDbiP02730
PeptideAtlasiP02730
PRIDEiP02730
ProteomicsDBi51557

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262418; ENSP00000262418; ENSG00000004939 [P02730-1]
GeneIDi6521
KEGGihsa:6521
UCSCiuc002igf.5 human [P02730-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6521
DisGeNETi6521
EuPathDBiHostDB:ENSG00000004939.13

GeneCards: human genes, protein and diseases

More...
GeneCardsi
SLC4A1
HGNCiHGNC:11027 SLC4A1
HPAiCAB034438
HPA015584
HPA063911
MalaCardsiSLC4A1
MIMi109270 gene+phenotype
110500 phenotype
112010 phenotype
112050 phenotype
130600 phenotype
166900 phenotype
179800 phenotype
185020 phenotype
601550 phenotype
601551 phenotype
611162 phenotype
611590 phenotype
612653 phenotype
neXtProtiNX_P02730
OpenTargetsiENSG00000004939
Orphaneti93608 Autosomal dominant distal renal tubular acidosis
3202 Dehydrated hereditary stomatocytosis
93610 Distal renal tubular acidosis with anemia
398088 Hereditary cryohydrocytosis with normal stomatin
822 Hereditary spherocytosis
98868 Southeast Asian ovalocytosis
PharmGKBiPA35895

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1172 Eukaryota
ENOG410XPHD LUCA
GeneTreeiENSGT00940000157423
HOVERGENiHBG004326
InParanoidiP02730
KOiK06573
OMAiFIYEEQI
OrthoDBi265068at2759
PhylomeDBiP02730
TreeFamiTF313630

Enzyme and pathway databases

ReactomeiR-HSA-1237044 Erythrocytes take up carbon dioxide and release oxygen
R-HSA-1247673 Erythrocytes take up oxygen and release carbon dioxide
R-HSA-425381 Bicarbonate transporters
R-HSA-5619050 Defective SLC4A1 causes hereditary spherocytosis type 4 (HSP4), distal renal tubular acidosis (dRTA) and dRTA with hemolytic anemia (dRTA-HA)
SIGNORiP02730

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
SLC4A1 human
EvolutionaryTraceiP02730

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Band_3

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
6521
PMAP-CutDBiP02730

Protein Ontology

More...
PROi
PR:P02730

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000004939 Expressed in 131 organ(s), highest expression level in trabecular bone tissue
ExpressionAtlasiP02730 baseline and differential
GenevisibleiP02730 HS

Family and domain databases

Gene3Di3.40.930.10, 1 hit
InterProiView protein in InterPro
IPR001717 Anion_exchange
IPR002977 Anion_exchange_1
IPR018241 Anion_exchange_CS
IPR013769 Band3_cytoplasmic_dom
IPR011531 HCO3_transpt_C
IPR003020 HCO3_transpt_euk
IPR016152 PTrfase/Anion_transptr
PANTHERiPTHR11453 PTHR11453, 1 hit
PfamiView protein in Pfam
PF07565 Band_3_cyto, 1 hit
PF00955 HCO3_cotransp, 2 hits
PRINTSiPR00165 ANIONEXCHNGR
PR01187 ANIONEXHNGR1
PR01231 HCO3TRNSPORT
SUPFAMiSSF55804 SSF55804, 1 hit
TIGRFAMsiTIGR00834 ae, 1 hit
PROSITEiView protein in PROSITE
PS00219 ANION_EXCHANGER_1, 1 hit
PS00220 ANION_EXCHANGER_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiB3AT_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P02730
Secondary accession number(s): G4V2I6
, P78487, Q1ZZ45, Q4KKW9, Q4VB84, Q9UCY7, Q9UDJ1
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1990
Last modified: January 16, 2019
This is version 245 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Blood group antigen proteins
    Nomenclature of blood group antigens and list of entries
  2. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. UniProtKB entry view manual
    User manual for the UniProtKB entry view
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  8. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  9. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
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