Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P02730

- B3AT_HUMAN

UniProt

P02730 - B3AT_HUMAN

Protein

Band 3 anion transport protein

Gene

SLC4A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 198 (01 Oct 2014)
      Sequence version 3 (01 Apr 1990)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Enzyme regulationi

    Phenyl isothiocyanate inhibits anion transport in vitro.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei590 – 5901Important for anion transport
    Sitei681 – 6811Important for anion-proton cotransport

    GO - Molecular functioni

    1. anion:anion antiporter activity Source: UniProtKB
    2. anion transmembrane transporter activity Source: ProtInc
    3. ankyrin binding Source: BHF-UCL
    4. bicarbonate transmembrane transporter activity Source: UniProtKB
    5. chloride transmembrane transporter activity Source: UniProtKB
    6. inorganic anion exchanger activity Source: UniProtKB
    7. protein anchor Source: BHF-UCL
    8. protein binding Source: UniProtKB
    9. protein homodimerization activity Source: BHF-UCL

    GO - Biological processi

    1. anion transport Source: UniProtKB
    2. bicarbonate transport Source: UniProtKB
    3. cellular ion homeostasis Source: ProtInc
    4. chloride transmembrane transport Source: GOC
    5. chloride transport Source: UniProtKB
    6. ion transport Source: Reactome
    7. small molecule metabolic process Source: Reactome
    8. transmembrane transport Source: Reactome

    Keywords - Molecular functioni

    Blood group antigen

    Keywords - Biological processi

    Anion exchange, Ion transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_121329. Erythrocytes take up carbon dioxide and release oxygen.
    REACT_121380. Erythrocytes take up oxygen and release carbon dioxide.
    REACT_19298. Bicarbonate transporters.

    Protein family/group databases

    TCDBi2.A.31.1.1. the anion exchanger (ae) family.

    Names & Taxonomyi

    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
    Gene namesi
    Name:SLC4A1
    Synonyms:AE1, DI, EPB3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:11027. SLC4A1.

    Subcellular locationi

    Cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein
    Note: Detected in the erythrocyte cell membrane and on the basolateral membrane of alpha-intercalated cells in the collecting duct in the kidney.

    GO - Cellular componenti

    1. basolateral plasma membrane Source: UniProtKB
    2. blood microparticle Source: UniProt
    3. cortical cytoskeleton Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. integral component of membrane Source: UniProtKB
    6. integral component of plasma membrane Source: UniProtKB
    7. plasma membrane Source: Reactome
    8. Z disc Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Elliptocytosis 4 (EL4) [MIM:109270]: A Rhesus-unlinked form of hereditary elliptocytosis, a genetically heterogeneous, autosomal dominant hematologic disorder. It is characterized by variable hemolytic anemia and elliptical or oval red cell shape.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti400 – 4089Missing in EL4; increased rigidity of the erythrocyte membrane leading to increased resistance to shear stress and increased resistance to P.falciparum. 2 Publications
    VAR_000801
    Spherocytosis 4 (SPH4) [MIM:612653]: Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal.15 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti90 – 901E → K in SPH4; Cape Town. 1 Publication
    Corresponds to variant rs28929480 [ dbSNP | Ensembl ].
    VAR_013784
    Natural varianti130 – 1301G → R in SPH4; Fukoka. 1 Publication
    VAR_013785
    Natural varianti147 – 1471P → S in SPH4; Mondego. 1 Publication
    VAR_013786
    Natural varianti285 – 2851A → D in SPH4; Boston. 1 Publication
    VAR_013787
    Natural varianti327 – 3271P → R in SPH4; Tuscaloosa. 1 Publication
    Corresponds to variant rs28931583 [ dbSNP | Ensembl ].
    VAR_000800
    Natural varianti455 – 4551G → E in SPH4; Benesov. 1 Publication
    VAR_013789
    Natural varianti455 – 4551G → R in SPH4; Yamagata. 1 Publication
    VAR_058038
    Natural varianti488 – 4881V → M in SPH4; Coimbra; also in AR-dRTA. 2 Publications
    Corresponds to variant rs28931584 [ dbSNP | Ensembl ].
    VAR_013791
    Natural varianti490 – 4901R → C in SPH4; Bicetre I. 1 Publication
    VAR_013792
    Natural varianti490 – 4901R → H in SPH4; Pinhal. 1 Publication
    VAR_058039
    Natural varianti518 – 5181R → C in SPH4; Dresden. 1 Publication
    VAR_000802
    Natural varianti663 – 6631M → K in SPH4; Tambau. 1 Publication
    VAR_058042
    Natural varianti663 – 6631Missing in SPH4; Osnabruck II. 1 Publication
    VAR_000807
    Natural varianti687 – 6871L → P in SPH4. 1 Publication
    VAR_039293
    Natural varianti705 – 7051D → Y in SPH4. 1 Publication
    VAR_039294
    Natural varianti707 – 7071L → P in SPH4; Most. 1 Publication
    VAR_013804
    Natural varianti714 – 7141G → R in SPH4; Okinawa. 1 Publication
    VAR_013805
    Natural varianti731 – 7311S → P in SPH4. 1 Publication
    VAR_039295
    Natural varianti734 – 7341H → R in SPH4. 1 Publication
    VAR_039296
    Natural varianti760 – 7601R → Q in SPH4; Prague II. 3 Publications
    VAR_013806
    Natural varianti760 – 7601R → W in SPH4; Hradec Kralove. 2 Publications
    VAR_013807
    Natural varianti771 – 7711G → D in SPH4; Chur. 1 Publication
    VAR_013808
    Natural varianti783 – 7831I → N in SPH4; Napoli II. 1 Publication
    VAR_013809
    Natural varianti808 – 8081R → C in SPH4; Jablonec. 1 Publication
    VAR_013810
    Natural varianti808 – 8081R → H in SPH4; Nara. 1 Publication
    VAR_013811
    Natural varianti834 – 8341H → P in SPH4; Birmingham. 1 Publication
    VAR_013812
    Natural varianti837 – 8371T → A in SPH4; Tokyo. 1 Publication
    VAR_013813
    Natural varianti837 – 8371T → M in SPH4; Philadelphia. 3 Publications
    VAR_013814
    Natural varianti837 – 8371T → R in SPH4; Nagoya. 1 Publication
    VAR_058043
    Natural varianti870 – 8701R → W in SPH4; Prague III. 2 Publications
    Corresponds to variant rs28931585 [ dbSNP | Ensembl ].
    VAR_013816
    Renal tubular acidosis, distal, autosomal dominant (AD-dRTA) [MIM:179800]: An 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.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti589 – 5891R → C in AD-dRTA; reduced red cell sulfate transport and altered glycosylation of the red cell band 3 N-glycan chain. 1 Publication
    VAR_015104
    Natural varianti589 – 5891R → H in AD-dRTA. 2 Publications
    VAR_015105
    Natural varianti589 – 5891R → S in AD-dRTA. 1 Publication
    VAR_015106
    Natural varianti609 – 6091G → 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 Publication
    VAR_058041
    Natural varianti613 – 6131S → F in AD-dRTA; markedly increased red cell sulfate transport but almost normal red cell iodide transport. 1 Publication
    VAR_015107
    Natural varianti858 – 8581A → D in AD-dRTA; impairs expression at the cell membrane. 1 Publication
    VAR_015108
    Renal tubular acidosis, distal, with hemolytic anemia (dRTA-HA) [MIM:611590]: A 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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti602 – 6021R → P in dRTA-HA. 1 Publication
    VAR_039292
    Natural varianti701 – 7011G → D in dRTA-HA; impairs expression at the cell membrane. 2 Publications
    Corresponds to variant rs121912748 [ dbSNP | Ensembl ].
    VAR_015171
    Natural varianti850 – 8501Missing in dRTA-HA. 1 Publication
    VAR_015109
    Renal tubular acidosis, distal, with normal red cell morphology (dRTA-NRC) [MIM:611590]: A 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti773 – 7731S → P in dRTA-NRC. 1 Publication
    VAR_039297

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi85 – 851E → A or R: Impairs expression at the cell membrane. 1 Publication
    Mutagenesisi283 – 2831R → A, E or S: Impairs expression at the cell membrane. 1 Publication
    Mutagenesisi642 – 6421N → D: Loss of N-glycosylation site. 1 Publication
    Mutagenesisi681 – 6811E → Q: Impairs expression at the cell membrane. 1 Publication

    Keywords - Diseasei

    Disease mutation, Elliptocytosis, Hereditary hemolytic anemia

    Organism-specific databases

    MIMi109270. gene+phenotype.
    110500. phenotype.
    112010. phenotype.
    112050. phenotype.
    130600. phenotype.
    179800. phenotype.
    601550. phenotype.
    601551. phenotype.
    611162. phenotype.
    611590. phenotype.
    612653. phenotype.
    Orphaneti93608. Autosomal dominant distal renal tubular acidosis.
    93610. Distal renal tubular acidosis with anemia.
    822. Hereditary spherocytosis.
    98868. Southeast Asian ovalocytosis.
    PharmGKBiPA35895.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 911911Band 3 anion transport proteinPRO_0000079209Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei8 – 81Phosphotyrosine2 Publications
    Modified residuei21 – 211Phosphotyrosine2 Publications
    Modified residuei46 – 461Phosphotyrosine1 Publication
    Modified residuei359 – 3591Phosphotyrosine1 Publication
    Glycosylationi642 – 6421N-linked (GlcNAc...) (complex)2 Publications
    Lipidationi843 – 8431S-palmitoyl cysteine1 Publication
    Modified residuei904 – 9041Phosphotyrosine1 Publication

    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

    Keywords - PTMi

    Acetylation, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    PaxDbiP02730.
    PRIDEiP02730.

    PTM databases

    PhosphoSiteiP02730.

    Miscellaneous databases

    PMAP-CutDBP02730.

    Expressioni

    Tissue specificityi

    Detected in erythrocytes (at protein level). Erythrocytes.3 Publications

    Gene expression databases

    BgeeiP02730.
    GenevestigatoriP02730.

    Organism-specific databases

    HPAiHPA015584.

    Interactioni

    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.4 Publications

    Protein-protein interaction databases

    BioGridi112412. 11 interactions.
    IntActiP02730. 2 interactions.
    MINTiMINT-1344291.
    STRINGi9606.ENSP00000262418.

    Structurei

    Secondary structure

    1
    911
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 124
    Beta strandi58 – 669
    Beta strandi68 – 703
    Beta strandi73 – 8816
    Beta strandi90 – 923
    Helixi104 – 11512
    Beta strandi118 – 1236
    Helixi128 – 14114
    Helixi147 – 1493
    Helixi150 – 1578
    Helixi164 – 1696
    Beta strandi173 – 1753
    Beta strandi188 – 1903
    Helixi195 – 2006
    Helixi212 – 2198
    Beta strandi226 – 2349
    Beta strandi241 – 25111
    Beta strandi256 – 2583
    Beta strandi262 – 2709
    Helixi278 – 29013
    Helixi292 – 3009
    Helixi304 – 31613
    Beta strandi319 – 3213
    Helixi329 – 3324
    Helixi333 – 3353
    Helixi336 – 34712
    Turni392 – 3943
    Helixi395 – 3995
    Helixi409 – 42214
    Helixi437 – 45317
    Turni806 – 8094
    Helixi829 – 8335

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP02730.
    SMRiP02730. Positions 55-356, 389-430, 803-835.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02730.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 403403CytoplasmicAdd
    BLAST
    Topological domaini542 – 56827ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini589 – 60315CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini625 – 66036ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei404 – 42421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei437 – 45620HelicalSequence AnalysisAdd
    BLAST
    Transmembranei460 – 47920HelicalSequence AnalysisAdd
    BLAST
    Transmembranei491 – 51020HelicalSequence AnalysisAdd
    BLAST
    Transmembranei523 – 54119HelicalSequence AnalysisAdd
    BLAST
    Transmembranei569 – 58820HelicalSequence AnalysisAdd
    BLAST
    Transmembranei604 – 62421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei661 – 68020HelicalSequence AnalysisAdd
    BLAST
    Transmembranei699 – 71921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei763 – 78018HelicalSequence AnalysisAdd
    BLAST
    Transmembranei785 – 80622HelicalSequence AnalysisAdd
    BLAST
    Transmembranei844 – 86522HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni55 – 290236GlobularAdd
    BLAST
    Regioni176 – 18510Interaction with ANK1Curated
    Regioni304 – 35754Dimerization armAdd
    BLAST
    Regioni404 – 911508Membrane (anion exchange)Add
    BLAST
    Regioni559 – 63072Involved in anion transportAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG268067.
    HOVERGENiHBG004326.
    InParanoidiP02730.
    KOiK06573.
    OMAiEYDEVAM.
    OrthoDBiEOG7TMZR0.
    PhylomeDBiP02730.
    TreeFamiTF313630.

    Family and domain databases

    Gene3Di3.40.1100.10. 1 hit.
    InterProiIPR001717. 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.
    [Graphical view]
    PANTHERiPTHR11453. PTHR11453. 1 hit.
    PfamiPF07565. Band_3_cyto. 1 hit.
    PF00955. HCO3_cotransp. 2 hits.
    [Graphical view]
    PRINTSiPR00165. ANIONEXCHNGR.
    PR01187. ANIONEXHNGR1.
    PR01231. HCO3TRNSPORT.
    SUPFAMiSSF55804. SSF55804. 1 hit.
    TIGRFAMsiTIGR00834. ae. 1 hit.
    PROSITEiPS00219. ANION_EXCHANGER_1. 1 hit.
    PS00220. ANION_EXCHANGER_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P02730-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEELQDDYED MMEENLEQEE YEDPDIPESQ MEEPAAHDTE ATATDYHTTS    50
    HPGTHKVYVE LQELVMDEKN QELRWMEAAR WVQLEENLGE NGAWGRPHLS 100
    HLTFWSLLEL RRVFTKGTVL LDLQETSLAG VANQLLDRFI FEDQIRPQDR 150
    EELLRALLLK HSHAGELEAL GGVKPAVLTR SGDPSQPLLP QHSSLETQLF 200
    CEQGDGGTEG HSPSGILEKI PPDSEATLVL VGRADFLEQP VLGFVRLQEA 250
    AELEAVELPV PIRFLFVLLG PEAPHIDYTQ LGRAAATLMS ERVFRIDAYM 300
    AQSRGELLHS LEGFLDCSLV LPPTDAPSEQ ALLSLVPVQR ELLRRRYQSS 350
    PAKPDSSFYK GLDLNGGPDD PLQQTGQLFG GLVRDIRRRY PYYLSDITDA 400
    FSPQVLAAVI FIYFAALSPA ITFGGLLGEK TRNQMGVSEL LISTAVQGIL 450
    FALLGAQPLL VVGFSGPLLV FEEAFFSFCE TNGLEYIVGR VWIGFWLILL 500
    VVLVVAFEGS FLVRFISRYT QEIFSFLISL IFIYETFSKL IKIFQDHPLQ 550
    KTYNYNVLMV PKPQGPLPNT ALLSLVLMAG TFFFAMMLRK FKNSSYFPGK 600
    LRRVIGDFGV PISILIMVLV DFFIQDTYTQ KLSVPDGFKV SNSSARGWVI 650
    HPLGLRSEFP IWMMFASALP ALLVFILIFL ESQITTLIVS KPERKMVKGS 700
    GFHLDLLLVV GMGGVAALFG MPWLSATTVR SVTHANALTV MGKASTPGAA 750
    AQIQEVKEQR ISGLLVAVLV GLSILMEPIL SRIPLAVLFG IFLYMGVTSL 800
    SGIQLFDRIL LLFKPPKYHP DVPYVKRVKT WRMHLFTGIQ IICLAVLWVV 850
    KSTPASLALP FVLILTVPLR RVLLPLIFRN VELQCLDADD AKATFDEEEG 900
    RDEYDEVAMP V 911
    Length:911
    Mass (Da):101,792
    Last modified:April 1, 1990 - v3
    Checksum:i35EC3EE7AFF27D2F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111M → D AA sequence (PubMed:6345535)Curated
    Sequence conflicti68 – 681E → EE AA sequence (PubMed:6345535)Curated
    Sequence conflicti759 – 7591Q → H in ABD74692. (PubMed:16252102)Curated

    Polymorphismi

    SLC4A1 is responsible for the Diego blood group system. 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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti27 – 271P → H.1 Publication
    Corresponds to variant rs55777403 [ dbSNP | Ensembl ].
    VAR_058035
    Natural varianti38 – 381D → A.4 Publications
    Corresponds to variant rs5035 [ dbSNP | Ensembl ].
    VAR_014612
    Natural varianti40 – 401E → K in hemolytic anemia; Montefiore. 2 Publications
    Corresponds to variant rs45562031 [ dbSNP | Ensembl ].
    VAR_000798
    Natural varianti45 – 451D → E.
    Corresponds to variant rs34700496 [ dbSNP | Ensembl ].
    VAR_036693
    Natural varianti56 – 561K → E in Di(a)/Memphis-II antigen. 5 Publications
    Corresponds to variant rs5036 [ dbSNP | Ensembl ].
    VAR_000799
    Natural varianti68 – 681E → K.
    Corresponds to variant rs13306787 [ dbSNP | Ensembl ].
    VAR_039290
    Natural varianti72 – 721E → D.1 Publication
    Corresponds to variant rs13306788 [ dbSNP | Ensembl ].
    VAR_058036
    Natural varianti73 – 731L → M.1 Publication
    VAR_039291
    Natural varianti90 – 901E → K in SPH4; Cape Town. 1 Publication
    Corresponds to variant rs28929480 [ dbSNP | Ensembl ].
    VAR_013784
    Natural varianti112 – 1121R → S.
    Corresponds to variant rs5037 [ dbSNP | Ensembl ].
    VAR_014613
    Natural varianti130 – 1301G → R in SPH4; Fukoka. 1 Publication
    VAR_013785
    Natural varianti147 – 1471P → S in SPH4; Mondego. 1 Publication
    VAR_013786
    Natural varianti285 – 2851A → D in SPH4; Boston. 1 Publication
    VAR_013787
    Natural varianti327 – 3271P → R in SPH4; Tuscaloosa. 1 Publication
    Corresponds to variant rs28931583 [ dbSNP | Ensembl ].
    VAR_000800
    Natural varianti400 – 4089Missing in EL4; increased rigidity of the erythrocyte membrane leading to increased resistance to shear stress and increased resistance to P.falciparum. 2 Publications
    VAR_000801
    Natural varianti429 – 4291E → D in NFLD+ antigen. 1 Publication
    VAR_058037
    Natural varianti432 – 4321R → W in ELO antigen.
    VAR_013788
    Natural varianti442 – 4421I → F.
    Corresponds to variant rs5018 [ dbSNP | Ensembl ].
    VAR_014614
    Natural varianti455 – 4551G → E in SPH4; Benesov. 1 Publication
    VAR_013789
    Natural varianti455 – 4551G → R in SPH4; Yamagata. 1 Publication
    VAR_058038
    Natural varianti480 – 4801E → K in FR(a+) antigen. 1 Publication
    VAR_013790
    Natural varianti488 – 4881V → M in SPH4; Coimbra; also in AR-dRTA. 2 Publications
    Corresponds to variant rs28931584 [ dbSNP | Ensembl ].
    VAR_013791
    Natural varianti490 – 4901R → C in SPH4; Bicetre I. 1 Publication
    VAR_013792
    Natural varianti490 – 4901R → H in SPH4; Pinhal. 1 Publication
    VAR_058039
    Natural varianti508 – 5081E → K.1 Publication
    Corresponds to variant rs45568837 [ dbSNP | Ensembl ].
    VAR_025090
    Natural varianti518 – 5181R → C in SPH4; Dresden. 1 Publication
    VAR_000802
    Natural varianti548 – 5481P → L in RB(A) antigen.
    VAR_000803
    Natural varianti551 – 5511K → N in TR(A) antigen.
    VAR_013793
    Natural varianti552 – 5521T → I in WARR antigen.
    VAR_000804
    Natural varianti555 – 5551Y → H in VG(a) antigen.
    VAR_013794
    Natural varianti557 – 5571V → M in WD(a) antigen.
    VAR_000805
    Natural varianti561 – 5611P → A in NFLD+ antigen. 1 Publication
    VAR_058040
    Natural varianti561 – 5611P → S in BOW antigen. 1 Publication
    VAR_013795
    Natural varianti565 – 5651G → A in WU antigen.
    VAR_013796
    Natural varianti566 – 5661P → A in KREP antigen.
    VAR_013797
    Natural varianti566 – 5661P → S in PN(a) antigen.
    VAR_013798
    Natural varianti569 – 5691N → K in BP(a) antigen.
    VAR_013799
    Natural varianti586 – 5861M → L.
    Corresponds to variant rs5019 [ dbSNP | Ensembl ].
    VAR_014615
    Natural varianti589 – 5891R → C in AD-dRTA; reduced red cell sulfate transport and altered glycosylation of the red cell band 3 N-glycan chain. 1 Publication
    VAR_015104
    Natural varianti589 – 5891R → H in AD-dRTA. 2 Publications
    VAR_015105
    Natural varianti589 – 5891R → S in AD-dRTA. 1 Publication
    VAR_015106
    Natural varianti602 – 6021R → P in dRTA-HA. 1 Publication
    VAR_039292
    Natural varianti609 – 6091G → 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 Publication
    VAR_058041
    Natural varianti613 – 6131S → F in AD-dRTA; markedly increased red cell sulfate transport but almost normal red cell iodide transport. 1 Publication
    VAR_015107
    Natural varianti646 – 6461R → Q in SW(a+) antigen. 1 Publication
    VAR_013800
    Natural varianti646 – 6461R → W in SW(a+) antigen. 1 Publication
    VAR_013801
    Natural varianti656 – 6561R → C in HG(a) antigen.
    VAR_013802
    Natural varianti656 – 6561R → H in MO(a) antigen.
    VAR_013803
    Natural varianti658 – 6581E → K in WR(a) antigen. 1 Publication
    VAR_000806
    Natural varianti663 – 6631M → K in SPH4; Tambau. 1 Publication
    VAR_058042
    Natural varianti663 – 6631Missing in SPH4; Osnabruck II. 1 Publication
    VAR_000807
    Natural varianti687 – 6871L → P in SPH4. 1 Publication
    VAR_039293
    Natural varianti688 – 6881I → V.
    Corresponds to variant rs5022 [ dbSNP | Ensembl ].
    VAR_014616
    Natural varianti690 – 6901S → G.
    Corresponds to variant rs5023 [ dbSNP | Ensembl ].
    VAR_014617
    Natural varianti701 – 7011G → D in dRTA-HA; impairs expression at the cell membrane. 2 Publications
    Corresponds to variant rs121912748 [ dbSNP | Ensembl ].
    VAR_015171
    Natural varianti705 – 7051D → Y in SPH4. 1 Publication
    VAR_039294
    Natural varianti707 – 7071L → P in SPH4; Most. 1 Publication
    VAR_013804
    Natural varianti714 – 7141G → R in SPH4; Okinawa. 1 Publication
    VAR_013805
    Natural varianti731 – 7311S → P in SPH4. 1 Publication
    VAR_039295
    Natural varianti734 – 7341H → R in SPH4. 1 Publication
    VAR_039296
    Natural varianti760 – 7601R → Q in SPH4; Prague II. 3 Publications
    VAR_013806
    Natural varianti760 – 7601R → W in SPH4; Hradec Kralove. 2 Publications
    VAR_013807
    Natural varianti771 – 7711G → D in SPH4; Chur. 1 Publication
    VAR_013808
    Natural varianti773 – 7731S → P in dRTA-NRC. 1 Publication
    VAR_039297
    Natural varianti783 – 7831I → N in SPH4; Napoli II. 1 Publication
    VAR_013809
    Natural varianti808 – 8081R → C in SPH4; Jablonec. 1 Publication
    VAR_013810
    Natural varianti808 – 8081R → H in SPH4; Nara. 1 Publication
    VAR_013811
    Natural varianti832 – 8321R → H.
    Corresponds to variant rs5025 [ dbSNP | Ensembl ].
    VAR_014618
    Natural varianti834 – 8341H → P in SPH4; Birmingham. 1 Publication
    VAR_013812
    Natural varianti837 – 8371T → A in SPH4; Tokyo. 1 Publication
    VAR_013813
    Natural varianti837 – 8371T → M in SPH4; Philadelphia. 3 Publications
    VAR_013814
    Natural varianti837 – 8371T → R in SPH4; Nagoya. 1 Publication
    VAR_058043
    Natural varianti850 – 8501Missing in dRTA-HA. 1 Publication
    VAR_015109
    Natural varianti854 – 8541P → L in Di(a)/Memphis-II antigen. 2 Publications
    Corresponds to variant rs2285644 [ dbSNP | Ensembl ].
    VAR_000808
    Natural varianti858 – 8581A → D in AD-dRTA; impairs expression at the cell membrane. 1 Publication
    VAR_015108
    Natural varianti862 – 8621V → I.1 Publication
    Corresponds to variant rs5026 [ dbSNP | Ensembl ].
    VAR_014619
    Natural varianti868 – 8681P → L in acanthocytosis; slightly increases transporter activity; impairs expression at the cell membrane. 1 Publication
    VAR_013815
    Natural varianti870 – 8701R → W in SPH4; Prague III. 2 Publications
    Corresponds to variant rs28931585 [ dbSNP | Ensembl ].
    VAR_013816

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    PIRiA36218. B3HU.
    RefSeqiNP_000333.1. NM_000342.3.
    XP_005257649.1. XM_005257592.2.
    UniGeneiHs.443948.

    Genome annotation databases

    EnsembliENST00000262418; ENSP00000262418; ENSG00000004939.
    GeneIDi6521.
    KEGGihsa:6521.
    UCSCiuc002igf.4. human.

    Polymorphism databases

    DMDMi114787.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS11481.1.
    PIRi A36218. B3HU.
    RefSeqi NP_000333.1. NM_000342.3.
    XP_005257649.1. XM_005257592.2.
    UniGenei Hs.443948.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BH7 NMR - A 803-835 [» ]
    1BNX NMR - A 389-430 [» ]
    1BTQ NMR - A 405-424 [» ]
    1BTR NMR - A 405-424 [» ]
    1BTS NMR - A 436-456 [» ]
    1BTT NMR - A 436-456 [» ]
    1BZK NMR - A 389-430 [» ]
    1HYN X-ray 2.60 P/Q/R/S 1-379 [» ]
    2BTA NMR - A 1-15 [» ]
    2BTB NMR - A 1-15 [» ]
    3BTB NMR - A 1-15 [» ]
    4KY9 X-ray 2.23 A/P 51-356 [» ]
    ProteinModelPortali P02730.
    SMRi P02730. Positions 55-356, 389-430, 803-835.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112412. 11 interactions.
    IntActi P02730. 2 interactions.
    MINTi MINT-1344291.
    STRINGi 9606.ENSP00000262418.

    Protein family/group databases

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

    PTM databases

    PhosphoSitei P02730.

    Polymorphism databases

    DMDMi 114787.

    Proteomic databases

    PaxDbi P02730.
    PRIDEi P02730.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262418 ; ENSP00000262418 ; ENSG00000004939 .
    GeneIDi 6521.
    KEGGi hsa:6521.
    UCSCi uc002igf.4. human.

    Organism-specific databases

    CTDi 6521.
    GeneCardsi GC17M042337.
    HGNCi HGNC:11027. SLC4A1.
    HPAi HPA015584.
    MIMi 109270. gene+phenotype.
    110500. phenotype.
    112010. phenotype.
    112050. phenotype.
    130600. phenotype.
    179800. phenotype.
    601550. phenotype.
    601551. phenotype.
    611162. phenotype.
    611590. phenotype.
    612653. phenotype.
    neXtProti NX_P02730.
    Orphaneti 93608. Autosomal dominant distal renal tubular acidosis.
    93610. Distal renal tubular acidosis with anemia.
    822. Hereditary spherocytosis.
    98868. Southeast Asian ovalocytosis.
    PharmGKBi PA35895.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG268067.
    HOVERGENi HBG004326.
    InParanoidi P02730.
    KOi K06573.
    OMAi EYDEVAM.
    OrthoDBi EOG7TMZR0.
    PhylomeDBi P02730.
    TreeFami TF313630.

    Enzyme and pathway databases

    Reactomei REACT_121329. Erythrocytes take up carbon dioxide and release oxygen.
    REACT_121380. Erythrocytes take up oxygen and release carbon dioxide.
    REACT_19298. Bicarbonate transporters.

    Miscellaneous databases

    EvolutionaryTracei P02730.
    GeneWikii Band_3.
    GenomeRNAii 6521.
    NextBioi 25367.
    PMAP-CutDB P02730.
    PROi P02730.
    SOURCEi Search...

    Gene expression databases

    Bgeei P02730.
    Genevestigatori P02730.

    Family and domain databases

    Gene3Di 3.40.1100.10. 1 hit.
    InterProi 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.
    [Graphical view ]
    PANTHERi PTHR11453. PTHR11453. 1 hit.
    Pfami PF07565. Band_3_cyto. 1 hit.
    PF00955. HCO3_cotransp. 2 hits.
    [Graphical view ]
    PRINTSi PR00165. ANIONEXCHNGR.
    PR01187. ANIONEXHNGR1.
    PR01231. HCO3TRNSPORT.
    SUPFAMi SSF55804. SSF55804. 1 hit.
    TIGRFAMsi TIGR00834. ae. 1 hit.
    PROSITEi PS00219. ANION_EXCHANGER_1. 1 hit.
    PS00220. ANION_EXCHANGER_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequence."
      Tanner M.J.A., Martin P.G., High S.
      Biochem. J. 256:703-712(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Blood.
    2. "Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1)."
      Lux S.E., John K.M., Kopito R.R., Lodish H.F.
      Proc. Natl. Acad. Sci. U.S.A. 86:9089-9093(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Recessive distal renal tubular acidosis in Sarawak caused by AE1 mutations."
      Choo K.E., Nicoli T.K., Bruce L.J., Tanner M.J., Ruiz-Linares A., Wrong O.M.
      Pediatr. Nephrol. 21:212-217(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-38.
    4. "Novel anion exchanger-1 expression in Southeast Asian populations."
      Hsu K., Huang S.-Y., Chi N., Lin M.
      Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Blood.
    5. SeattleSNPs variation discovery resource
      Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-38; GLU-56; LYS-508 AND ILE-862.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-27.
      Tissue: Cerebellum.
    8. "Primary structure of the cytoplasmic domain of human erythrocyte protein band 3. Comparison with its sequence in the mouse."
      Yannoukakos D., Vasseur C., Blouquit Y., Bursaux E., Wajcman H.
      Biochim. Biophys. Acta 998:43-49(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-199; 220-292 AND 347-370, ACETYLATION AT MET-1.
    9. "Amino acid sequence of the N alpha-terminal 201 residues of human erythrocyte membrane band 3."
      Kaul R.K., Murthy S.N.P., Reddy A.G., Steck T.L., Kohler H.
      J. Biol. Chem. 258:7981-7990(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-201.
    10. "Orientation of the band 3 polypeptide from human erythrocyte membranes. Identification of NH2-terminal sequence and site of carbohydrate attachment."
      Drickamer L.K.
      J. Biol. Chem. 253:7242-7248(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-3.
    11. "Anion exchanger 1 in human kidney and oncocytoma differs from erythroid AE1 in its NH2 terminus."
      Kollert-Jons A., Wagner S., Hubner S., Appelhans H., Drenckhahn D.
      Am. J. Physiol. 265:F813-F821(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 66-180.
    12. "A structural study of the membrane domain of band 3 by tryptic digestion. Conformational change of band 3 in situ induced by alkali treatment."
      Kang D., Okubo K., Hamasaki N., Kuroda N., Shiraki H.
      J. Biol. Chem. 267:19211-19217(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 361-372; 390-399; 604-613; 632-639; 647-656; 699-729; 731-743; 761-781 AND 818-826, SYNTHESIS OF 646-656 AND 817-827.
    13. "The human erythrocyte anion-transport protein. Partial amino acid sequence, conformation and a possible molecular mechanism for anion exchange."
      Brock C.J., Tanner M.J.A., Kempf C.
      Biochem. J. 213:577-586(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 559-630.
    14. "Anion-proton cotransport through the human red blood cell band 3 protein. Role of glutamate 681."
      Jennings M.L., Smith J.S.
      J. Biol. Chem. 267:13964-13971(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 665-688, ROLE OF GLU-681.
    15. "Band 3 Chur: a variant associated with band 3-deficient hereditary spherocytosis and substitution in a highly conserved position of transmembrane segment 11."
      Maillet P., Vallier A., Reinhart W.H., Wyss E.J., Ott P., Texier P., Baklouti F., Tanner M.J.A., Delaunay J., Alloisio N.
      Br. J. Haematol. 91:804-810(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 757-778, VARIANT SPH4 ASP-771.
    16. "Localization of the pyridoxal phosphate binding site at the COOH-terminal region of erythrocyte band 3 protein."
      Kawano Y., Okubo K., Tokunaga F., Miyata T., Iwanaga S., Hamasaki N.
      J. Biol. Chem. 263:8232-8238(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 834-911.
    17. Cited for: PHOSPHORYLATION AT TYR-8; TYR-21 AND TYR-46.
    18. "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."
      Okubo K., Hamasaki N., Hara K., Kageura M.
      J. Biol. Chem. 266:16420-16424(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-843.
    19. "The ANK repeats of erythrocyte ankyrin form two distinct but cooperative binding sites for the erythrocyte anion exchanger."
      Michaely P., Bennett V.
      J. Biol. Chem. 270:22050-22057(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANK1.
    20. "Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein."
      Li J., Quilty J., Popov M., Reithmeier R.A.
      Biochem. J. 349:51-57(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-642.
    21. "Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine kinases in intact human erythrocytes: identification of primary and secondary phosphorylation sites."
      Brunati A.M., Bordin L., Clari G., James P., Quadroni M., Baritono E., Pinna L.A., Donella-Deana A.
      Blood 96:1550-1557(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-8; TYR-21; TYR-359 AND TYR-904.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains."
      Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R.
      Biochim. Biophys. Acta 1828:956-966(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH STOM, SUBUNIT.
    24. "Two-dimensional structure of the membrane domain of human band 3, the anion transport protein of the erythrocyte membrane."
      Wang D.N., Kuehlbrandt W., Sarabia V.E., Reithmeier R.A.F.
      EMBO J. 12:2233-2239(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON CRYOMICROSCOPY.
    25. "Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3."
      Wang D.N., Sarabia V.E., Reithmeier R.A.F., Kuehlbrandt W.
      EMBO J. 13:3230-3235(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON CRYOMICROSCOPY.
    26. "The solution structures of the first and second transmembrane-spanning segments of band 3."
      Gargaro A.R., Bloomberg G.B., Dempsey C.E., Murray M., Tanner M.J.A.
      Eur. J. Biochem. 221:445-454(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 405-424 AND 436-456.
    27. "Solution structure of a band 3 peptide inhibitor bound to aldolase: a proposed mechanism for regulating binding by tyrosine phosphorylation."
      Schneider M.L., Post C.B.
      Biochemistry 34:16574-16584(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-16.
    28. "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."
      Eisenmesser E.Z., Post C.B.
      Biochemistry 37:867-877(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-16.
    29. "Studies on the structure of a transmembrane region and a cytoplasmic loop of the human red cell anion exchanger."
      Chambers E.J., Askin D., Bloomberg G.B., Ring S.M., Tanner M.J.
      Biochem. Soc. Trans. 26:516-520(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 389-430.
    30. "NMR solution structure of a cytoplasmic surface loop of the human red cell anion transporter, band 3."
      Askin D., Bloomberg G.B., Chambers E.J., Tanner M.J.
      Biochemistry 37:11670-11678(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 803-835.
    31. "Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3."
      Zhang D., Kiyatkin A., Bolin J.T., Low P.S.
      Blood 96:2925-2933(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-379, SUBUNIT.
    32. "A substrate access tunnel in the cytosolic domain is not an essential feature of the solute carrier 4 (SLC4) family of bicarbonate transporters."
      Shnitsar V., Li J., Li X., Calmettes C., Basu A., Casey J.R., Moraes T.F., Reithmeier R.A.
      J. Biol. Chem. 288:33848-33860(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 51-356, FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-642, MUTAGENESIS OF GLU-85; ARG-283; ASN-642 AND GLU-681, CHARACTERIZATION OF VARIANT ACANTHOCYTOSIS LEU-868.
    33. "Human erythrocyte band 3 polymorphism (band 3 Memphis): characterization of the structural modification (Lys 56-->Glu) by protein chemistry methods."
      Yannoukakos D., Vasseur C., Driancourt C., Blouquit Y., Delauney J., Wajcman H., Bursaux E.
      Blood 78:1117-1120(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MEMPHIS GLU-56.
    34. "Deletion in erythrocyte band 3 gene in malaria-resistant Southeast Asian ovalocytosis."
      Jarolim P., Palek J., Amato D., Hassan K., Sapak P., Nurse G.T., Rubin H.L., Zhai S., Sahr K.E., Liu S.-C.
      Proc. Natl. Acad. Sci. U.S.A. 88:11022-11026(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EL4 400-ALA--ALA-408 DEL, VARIANT MEMPHIS GLU-56.
    35. "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."
      Jarolim P., Palek J., Rubin H.L., Prchal J.T., Korsgren C., Cohen C.M.
      Blood 80:523-529(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SPH4 ARG-327.
    36. Cited for: VARIANT EL4 400-ALA--ALA-408 DEL, CHARACTERIZATION OF VARIANT EL4 400-ALA--ALA-408 DEL, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    37. "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."
      Bruce L.J., Kay M.M., Lawrence C., Tanner M.J.
      Biochem. J. 293:317-320(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ACANTHOCYTOSIS LEU-868.
    38. "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)."
      Rybicki A.C., Qiu J.J.H., Musto S., Rosen N.L., Nagel R.L., Schwartz R.S.
      Blood 81:2155-2165(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HEMOLYTIC ANEMIA LYS-40.
    39. "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."
      Bruce L.J., Anstee D.J., Spring F.A., Tanner M.J.
      J. Biol. Chem. 269:16155-16158(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BLOOD GROUP DI(A)/MEMPHIS-II GLU-56 AND LEU-854.
    40. "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."
      Bruce L.J., Ring S.M., Anstee D.J., Reid M.E., Wilkinson S., Tanner M.J.
      Blood 85:541-547(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BLOOD GROUP WR(A) LYS-658.
    41. "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."
      Jarolim P., Rubin H.L., Brabec V., Chrobak L., Zolotarev A.S., Alper S.L., Brugnara C., Wichterle H., Palek J.
      Blood 85:634-640(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SPH4 GLN-760; TRP-760; CYS-808 AND TRP-870.
    42. "Characterization of 13 novel band 3 gene defects in hereditary spherocytosis with band 3 deficiency."
      Jarolim P., Murray J.L., Rubin H.L., Taylor W.M., Prchal J.T., Ballas S.K., Snyder L.M., Chrobak L., Melrose W.D., Brabec V., Palek J.
      Blood 88:4366-4374(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SPH4 ASP-285; GLU-455; PRO-707; PRO-834 AND MET-837.
    43. Cited for: VARIANTS SPH4 LYS-40; CYS-518 AND MET-663 DEL.
    44. "Modulation of clinical expression and band 3 deficiency in hereditary spherocytosis."
      Alloisio N., Texier P., Vallier A., Ribeiro M.L., Morle L., Bozon M., Bursaux E., Maillet P., Goncalves P., Tanner M.J., Tamagnini G., Delaunay J.
      Blood 90:414-420(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SPH4 SER-147 AND MET-488.
    45. "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."
      Miraglia del Giudice E., Vallier A., Maillet P., Perrotta S., Cutillo S., Iolascon A., Tanner M.J., Delaunay J., Alloisio N.
      Br. J. Haematol. 96:70-76(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SPH4 ASN-783, VARIANTS ALA-38 AND MET-73.
    46. "Heterogenous band 3 deficiency in hereditary spherocytosis related to different band 3 gene defects."
      Dhermy D., Galand C., Bournier O., Boulanger L., Cynober T., Schismanoff P.O., Bursaux E., Tchernia G., Boivin P., Garbarz M.
      Br. J. Haematol. 98:32-40(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SPH4 CYS-490 AND MET-837.
    47. "Familial distal renal tubular acidosis is associated with mutations in the red cell anion exchanger (Band 3, AE1) gene."
      Bruce L.J., Cope D.L., Jones G.K., Schofield A.E., Burley M., Povey S., Unwin R.J., Wrong O., Tanner M.J.
      J. Clin. Invest. 100:1693-1707(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS AD-DRTA CYS-589; HIS-589 AND PHE-613.
    48. "Blood group antigens Rb(a), Tr(a), and Wd(a) are located in the third ectoplasmic loop of erythroid band 3."
      Jarolim P., Murray J.L., Rubin H.L., Smart E., Moulds J.M.
      Transfusion 37:607-615(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BLOOD GROUPS RB(A); TR(A) AND WD(A).
    49. "Band 3 Tokyo: Thr837-->Ala837 substitution in erythrocyte band 3 protein associated with spherocytic hemolysis."
      Iwase S., Ideguchi H., Takao M., Horiguchi-Yamada J., Iwasaki M., Takahara S., Sekikawa T., Mochizuki S., Yamada H.
      Acta Haematol. 100:200-203(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SPH4 ALA-837.
    50. "Characterization of seven low incidence blood group antigens carried by erythrocyte band 3 protein."
      Jarolim P., Rubin H.L., Zakova D., Storry J., Reid M.E.
      Blood 92:4836-4843(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BLOOD GROUPS BOW; BP(A); ELO; HG(A); MO(A); VG(A) AND WU.
    51. "Novel AE1 mutations in recessive distal renal tubular acidosis: loss-of-function is rescued by glycophorin A."
      Tanphaichitr V.S., Sumboonnanonda A., Ideguchi H., Shayakul C., Brugnara C., Takao M., Veerakul G., Alper S.L.
      J. Clin. Invest. 102:2173-2179(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DRTA-HA ASP-701.
    52. "Mutations in the chloride-bicarbonate exchanger gene AE1 cause autosomal dominant but not autosomal recessive distal renal tubular acidosis."
      Karet F.E., Gainza F.J., Gyory A.Z., Unwin R.J., Wrong O., Tanner M.J.A., Nayir A., Alpay H., Santos F., Hulton S.A., Bakkaloglu A., Ozen S., Cunningham M.J., di Pietro A., Walker W.G., Lifton R.P.
      Proc. Natl. Acad. Sci. U.S.A. 95:6337-6342(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS AD-DRTA HIS-589 AND SER-589.
    53. "A Gly565-->Ala substitution in human erythroid band 3 accounts for the Wu blood group polymorphism."
      Zelinski T., McManus K., Punter F., Moulds M., Coghlan G.
      Transfusion 38:745-748(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BLOOD GROUP WU.
    54. "Arginine 490 is a hot spot for mutation in the band 3 gene in hereditary spherocytosis."
      Lima P.R.M., Sales T.S.I., Costa F.F., Saad S.T.O.
      Eur. J. Haematol. 63:360-361(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SPH4 HIS-490.
    55. "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."
      Bruce L.J., Wrong O., Toye A.M., Young M.T., Ogle G., Ismail Z., Sinha A.K., McMaster P., Hwaihwanje I., Nash G.B., Hart S., Lavu E., Palmer R., Othman A., Unwin R.J., Tanner M.J.A.
      Biochem. J. 350:41-51(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DRTA-HA ASP-701 AND VAL-850 DEL, VARIANT AD-DRTA ASP-858, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    56. "Severe hereditary spherocytosis and distal renal tubular acidosis associated with the total absence of band 3."
      Ribeiro M.L., Alloisio N., Almeida H., Gomes C., Texier P., Lemos C., Mimoso G., Morle L., Bey-Cabet F., Rudigoz R.-C., Delaunay J., Tamagnini G.
      Blood 96:1602-1604(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SPH4 MET-488.
    57. "Characteristic features of the genotype and phenotype of hereditary spherocytosis in the Japanese population."
      Yawata Y., Kanzaki A., Yawata A., Doerfler W., Oezcan R., Eber S.W.
      Int. J. Hematol. 71:118-135(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SPH4 ARG-130; ARG-455; ARG-714; TRP-760; GLN-760; HIS-808; ARG-837 AND MET-837, VARIANTS ALA-38; GLU-56; ASP-72 AND LEU-854.
    58. "Trafficking and folding defects in hereditary spherocytosis mutants of the human red cell anion exchanger."
      Quilty J.A., Reithmeier R.A.
      Traffic 1:987-998(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS PRO-707; GLN-760; TRP-760; CYS-808; PRO-834; MET-837 AND TRP-870.
    59. "Amino acid substitutions in human erythroid protein band 3 account for the low-incidence antigens NFLD and BOW."
      McManus K., Pongoski J., Coghlan G., Zelinski T.
      Transfusion 40:325-329(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BLOOD GROUP NFLD+ ASP-429 AND ALA-561, VARIANT BLOOD GROUP BOW+ SER-561.
    60. "An amino acid substitution in the putative second extracellular loop of RBC band 3 accounts for the Froese blood group polymorphism."
      McManus K., Lupe K., Coghlan G., Zelinski T.
      Transfusion 40:1246-1249(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BLOOD GROUP FR(A+) LYS-480.
    61. "Distinctive Swann blood group genotypes: molecular investigations."
      Zelinski T., Rusnak A., McManus K., Coghlan G.
      Vox Sang. 79:215-218(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BLOOD GROUP SW(A+) GLN-646 AND TRP-646.
    62. "Band 3 Cape Town (E90K) causes severe hereditary spherocytosis in combination with band 3 Prague III."
      Bracher N.A., Lyons C.A., Wessels G., Mansvelt E., Coetzer T.L.
      Br. J. Haematol. 113:689-693(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SPH4 LYS-90 AND TRP-870.
    63. "Novel compound heterozygous SLC4A1 mutations in Thai patients with autosomal recessive distal renal tubular acidosis."
      Sritippayawan S., Sumboonnanonda A., Vasuvattakul S., Keskanokwong T., Sawasdee N., Paemanee A., Thuwajit P., Wilairat P., Nimmannit S., Malasit P., Yenchitsomanus P.T.
      Am. J. Kidney Dis. 44:64-70(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DRTA-HA PRO-602, VARIANT DRTA-NRC PRO-773.
    64. "A novel missense mutation in AE1 causing autosomal dominant distal renal tubular acidosis retains normal transport function but is mistargeted in polarized epithelial cells."
      Rungroj N., Devonald M.A.J., Cuthbert A.W., Reimann F., Akkarapatumwong V., Yenchitsomanus P.-T., Bennett W.M., Karet F.E.
      J. Biol. Chem. 279:13833-13838(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AD-DRTA ARG-609, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT AD-DRTA ARG-609.
    65. "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."
      Lima P.R.M., Baratti M.O., Chiattone M.L., Costa F.F., Saad S.T.O.
      Eur. J. Haematol. 74:396-401(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SPH4 LYS-663.
    66. "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."
      Bruce L.J., Robinson H.C., Guizouarn H., Borgese F., Harrison P., King M.-J., Goede J.S., Coles S.E., Gore D.M., Lutz H.U., Ficarella R., Layton D.M., Iolascon A., Ellory J.C., Stewart G.W.
      Nat. Genet. 37:1258-1263(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SPH4 PRO-687; TYR-705; PRO-731; ARG-734 AND GLN-760.
    67. "Impaired trafficking and intracellular retention of mutant kidney anion exchanger 1 proteins (G701D and A858D) associated with distal renal tubular acidosis."
      Ungsupravate D., Sawasdee N., Khositseth S., Udomchaiprasertkul W., Khoprasert S., Li J., Reithmeier R.A., Yenchitsomanus P.T.
      Mol. Membr. Biol. 27:92-103(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT DRTA-HA ASP-701, CHARACTERIZATION OF VARIANT AD-DRTA ASP-858, SUBUNIT, SUBCELLULAR LOCATION, FUNCTION.

    Entry informationi

    Entry nameiB3AT_HUMAN
    AccessioniPrimary (citable) accession number: P02730
    Secondary accession number(s): G4V2I6
    , P78487, Q1ZZ45, Q4KKW9, Q4VB84, Q9UCY7, Q9UDJ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 198 of the entry and version 3 of the sequence. [Complete history]
    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.

    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. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    4. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    5. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    7. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    8. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3