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P02730 (B3AT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 196. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SLC4A1
Synonyms:AE1, DI, EPB3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length911 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.32 Ref.36 Ref.56 Ref.65 Ref.68

Enzyme regulation

Phenyl isothiocyanate inhibits anion transport in vitro.

Subunit structure

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. Ref.19 Ref.23 Ref.31 Ref.68

Subcellular location

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. Ref.23 Ref.32 Ref.36 Ref.56 Ref.65 Ref.68

Tissue specificity

Detected in erythrocytes (at protein level). Erythrocytes. Ref.23 Ref.36 Ref.56

Post-translational modification

Phosphorylated on Tyr-8 and Tyr-21 most likely by SYK. PP1-resistant phosphorylation that precedes Tyr-359 and Tyr-904 phosphorylation. Ref.17 Ref.21

Phosphorylated on Tyr-359 and Tyr-904 most likely by LYN. PP1-inhibited phosphorylation that follows Tyr-8 and Tyr-21 phosphorylation. Ref.17 Ref.21

Polymorphism

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) [MIM: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) [MIM: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 [MIM:611162].

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.34 Ref.36

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.35 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.50 Ref.55 Ref.57 Ref.58 Ref.63 Ref.66 Ref.67

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.

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the anion exchanger (TC 2.A.31) family. [View classification]

Ontologies

Keywords
   Biological processAnion exchange
Ion transport
Transport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Elliptocytosis
Hereditary hemolytic anemia
   DomainTransmembrane
Transmembrane helix
   Molecular functionBlood group antigen
   PTMAcetylation
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processanion transport

Inferred from direct assay Ref.65. Source: UniProtKB

bicarbonate transport

Inferred from direct assay Ref.32. Source: UniProtKB

cellular ion homeostasis

Traceable author statement PubMed 8841202. Source: ProtInc

chloride transmembrane transport

Inferred from sequence or structural similarity. Source: GOC

chloride transport

Inferred from sequence or structural similarity. Source: UniProtKB

ion transport

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentZ disc

Inferred from sequence or structural similarity. Source: UniProtKB

basolateral plasma membrane

Inferred from direct assay PubMed 12539048Ref.65. Source: UniProtKB

blood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

cortical cytoskeleton

Inferred from direct assay PubMed 16669616. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

integral component of membrane

Non-traceable author statement Ref.12. Source: UniProtKB

integral component of plasma membrane

Inferred from direct assay Ref.32. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionanion transmembrane transporter activity

Traceable author statement PubMed 4027230. Source: ProtInc

anion:anion antiporter activity

Inferred from direct assay Ref.65. Source: UniProtKB

ankyrin binding

Inferred from physical interaction PubMed 379653. Source: BHF-UCL

bicarbonate transmembrane transporter activity

Inferred from direct assay Ref.32. Source: UniProtKB

chloride transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

inorganic anion exchanger activity

Inferred from direct assay Ref.32. Source: UniProtKB

protein anchor

Traceable author statement PubMed 10950304. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 16669616. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction PubMed 379653. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 911911Band 3 anion transport protein
PRO_0000079209

Regions

Topological domain1 – 403403Cytoplasmic
Transmembrane404 – 42421Helical; Potential
Transmembrane437 – 45620Helical; Potential
Transmembrane460 – 47920Helical; Potential
Transmembrane491 – 51020Helical; Potential
Transmembrane523 – 54119Helical; Potential
Topological domain542 – 56827Extracellular Potential
Transmembrane569 – 58820Helical; Potential
Topological domain589 – 60315Cytoplasmic Potential
Transmembrane604 – 62421Helical; Potential
Topological domain625 – 66036Extracellular Potential
Transmembrane661 – 68020Helical; Potential
Transmembrane699 – 71921Helical; Potential
Transmembrane763 – 78018Helical; Potential
Transmembrane785 – 80622Helical; Potential
Transmembrane844 – 86522Helical; Potential
Region55 – 290236Globular
Region176 – 18510Interaction with ANK1 Probable
Region304 – 35754Dimerization arm
Region404 – 911508Membrane (anion exchange)
Region559 – 63072Involved in anion transport

Sites

Site5901Important for anion transport
Site6811Important for anion-proton cotransport

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8 Ref.10
Modified residue81Phosphotyrosine Ref.17 Ref.21
Modified residue211Phosphotyrosine Ref.17 Ref.21
Modified residue461Phosphotyrosine Ref.17
Modified residue3591Phosphotyrosine Ref.21
Modified residue9041Phosphotyrosine Ref.21
Lipidation8431S-palmitoyl cysteine Ref.18
Glycosylation6421N-linked (GlcNAc...) (complex) Ref.20 Ref.32

Natural variations

Natural variant271P → H. Ref.7
Corresponds to variant rs55777403 [ dbSNP | Ensembl ].
VAR_058035
Natural variant381D → A. Ref.3 Ref.5 Ref.45 Ref.58
Corresponds to variant rs5035 [ dbSNP | Ensembl ].
VAR_014612
Natural variant401E → K in hemolytic anemia; Montefiore. Ref.38 Ref.43
Corresponds to variant rs45562031 [ dbSNP | Ensembl ].
VAR_000798
Natural variant451D → E.
Corresponds to variant rs34700496 [ dbSNP | Ensembl ].
VAR_036693
Natural variant561K → E in Di(a)/Memphis-II antigen. Ref.5 Ref.33 Ref.34 Ref.39 Ref.58
Corresponds to variant rs5036 [ dbSNP | Ensembl ].
VAR_000799
Natural variant681E → K.
Corresponds to variant rs13306787 [ dbSNP | Ensembl ].
VAR_039290
Natural variant721E → D. Ref.58
Corresponds to variant rs13306788 [ dbSNP | Ensembl ].
VAR_058036
Natural variant731L → M. Ref.45
VAR_039291
Natural variant901E → K in SPH4; Cape Town. Ref.63
Corresponds to variant rs28929480 [ dbSNP | Ensembl ].
VAR_013784
Natural variant1121R → S.
Corresponds to variant rs5037 [ dbSNP | Ensembl ].
VAR_014613
Natural variant1301G → R in SPH4; Fukoka. Ref.58
VAR_013785
Natural variant1471P → S in SPH4; Mondego. Ref.44
VAR_013786
Natural variant2851A → D in SPH4; Boston. Ref.42
VAR_013787
Natural variant3271P → R in SPH4; Tuscaloosa. Ref.35
Corresponds to variant rs28931583 [ dbSNP | Ensembl ].
VAR_000800
Natural variant400 – 4089Missing in EL4; increased rigidity of the erythrocyte membrane leading to increased resistance to shear stress and increased resistance to P.falciparum.
VAR_000801
Natural variant4291E → D in NFLD+ antigen. Ref.60
VAR_058037
Natural variant4321R → W in ELO antigen.
VAR_013788
Natural variant4421I → F.
Corresponds to variant rs5018 [ dbSNP | Ensembl ].
VAR_014614
Natural variant4551G → E in SPH4; Benesov. Ref.42
VAR_013789
Natural variant4551G → R in SPH4; Yamagata. Ref.58
VAR_058038
Natural variant4801E → K in FR(a+) antigen. Ref.61
VAR_013790
Natural variant4881V → M in SPH4; Coimbra; also in AR-dRTA. Ref.44 Ref.57
Corresponds to variant rs28931584 [ dbSNP | Ensembl ].
VAR_013791
Natural variant4901R → C in SPH4; Bicetre I. Ref.46
VAR_013792
Natural variant4901R → H in SPH4; Pinhal. Ref.55
VAR_058039
Natural variant5081E → K. Ref.5
Corresponds to variant rs45568837 [ dbSNP | Ensembl ].
VAR_025090
Natural variant5181R → C in SPH4; Dresden. Ref.43
VAR_000802
Natural variant5481P → L in RB(A) antigen.
VAR_000803
Natural variant5511K → N in TR(A) antigen.
VAR_013793
Natural variant5521T → I in WARR antigen.
VAR_000804
Natural variant5551Y → H in VG(a) antigen.
VAR_013794
Natural variant5571V → M in WD(a) antigen.
VAR_000805
Natural variant5611P → A in NFLD+ antigen. Ref.60
VAR_058040
Natural variant5611P → S in BOW antigen. Ref.60
VAR_013795
Natural variant5651G → A in WU antigen.
VAR_013796
Natural variant5661P → A in KREP antigen.
VAR_013797
Natural variant5661P → S in PN(a) antigen.
VAR_013798
Natural variant5691N → K in BP(a) antigen.
VAR_013799
Natural variant5861M → L.
Corresponds to variant rs5019 [ dbSNP | Ensembl ].
VAR_014615
Natural variant5891R → C in AD-dRTA; reduced red cell sulfate transport and altered glycosylation of the red cell band 3 N-glycan chain. Ref.48
VAR_015104
Natural variant5891R → H in AD-dRTA. Ref.48 Ref.53
VAR_015105
Natural variant5891R → S in AD-dRTA. Ref.53
VAR_015106
Natural variant6021R → P in dRTA-HA. Ref.64
VAR_039292
Natural variant6091G → 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. Ref.65
VAR_058041
Natural variant6131S → F in AD-dRTA; markedly increased red cell sulfate transport but almost normal red cell iodide transport. Ref.48
VAR_015107
Natural variant6461R → Q in SW(a+) antigen. Ref.62
VAR_013800
Natural variant6461R → W in SW(a+) antigen. Ref.62
VAR_013801
Natural variant6561R → C in HG(a) antigen.
VAR_013802
Natural variant6561R → H in MO(a) antigen.
VAR_013803
Natural variant6581E → K in WR(a) antigen. Ref.40
VAR_000806
Natural variant6631M → K in SPH4; Tambau. Ref.66
VAR_058042
Natural variant6631Missing in SPH4; Osnabruck II. Ref.43
VAR_000807
Natural variant6871L → P in SPH4. Ref.67
VAR_039293
Natural variant6881I → V.
Corresponds to variant rs5022 [ dbSNP | Ensembl ].
VAR_014616
Natural variant6901S → G.
Corresponds to variant rs5023 [ dbSNP | Ensembl ].
VAR_014617
Natural variant7011G → D in dRTA-HA; impairs expression at the cell membrane. Ref.52 Ref.56 Ref.68
Corresponds to variant rs121912748 [ dbSNP | Ensembl ].
VAR_015171
Natural variant7051D → Y in SPH4. Ref.67
VAR_039294
Natural variant7071L → P in SPH4; Most. Ref.42 Ref.59
VAR_013804
Natural variant7141G → R in SPH4; Okinawa. Ref.58
VAR_013805
Natural variant7311S → P in SPH4. Ref.67
VAR_039295
Natural variant7341H → R in SPH4. Ref.67
VAR_039296
Natural variant7601R → Q in SPH4; Prague II. Ref.41 Ref.58 Ref.59 Ref.67
VAR_013806
Natural variant7601R → W in SPH4; Hradec Kralove. Ref.41 Ref.58 Ref.59
VAR_013807
Natural variant7711G → D in SPH4; Chur. Ref.15
VAR_013808
Natural variant7731S → P in dRTA-NRC. Ref.64
VAR_039297
Natural variant7831I → N in SPH4; Napoli II. Ref.45
VAR_013809
Natural variant8081R → C in SPH4; Jablonec. Ref.41 Ref.59
VAR_013810
Natural variant8081R → H in SPH4; Nara. Ref.58
VAR_013811
Natural variant8321R → H.
Corresponds to variant rs5025 [ dbSNP | Ensembl ].
VAR_014618
Natural variant8341H → P in SPH4; Birmingham. Ref.42 Ref.59
VAR_013812
Natural variant8371T → A in SPH4; Tokyo. Ref.50
VAR_013813
Natural variant8371T → M in SPH4; Philadelphia. Ref.42 Ref.46 Ref.58 Ref.59
VAR_013814
Natural variant8371T → R in SPH4; Nagoya. Ref.58
VAR_058043
Natural variant8501Missing in dRTA-HA. Ref.56
VAR_015109
Natural variant8541P → L in Di(a)/Memphis-II antigen. Ref.39 Ref.58
Corresponds to variant rs2285644 [ dbSNP | Ensembl ].
VAR_000808
Natural variant8581A → D in AD-dRTA; impairs expression at the cell membrane. Ref.56 Ref.68
VAR_015108
Natural variant8621V → I. Ref.5
Corresponds to variant rs5026 [ dbSNP | Ensembl ].
VAR_014619
Natural variant8681P → L in acanthocytosis; slightly increases transporter activity; impairs expression at the cell membrane. Ref.32 Ref.37
VAR_013815
Natural variant8701R → W in SPH4; Prague III. Ref.41 Ref.59 Ref.63
Corresponds to variant rs28931585 [ dbSNP | Ensembl ].
VAR_013816

Experimental info

Mutagenesis851E → A or R: Impairs expression at the cell membrane. Ref.32
Mutagenesis2831R → A, E or S: Impairs expression at the cell membrane. Ref.32
Mutagenesis6421N → D: Loss of N-glycosylation site. Ref.32
Mutagenesis6811E → Q: Impairs expression at the cell membrane. Ref.32
Sequence conflict111M → D AA sequence Ref.9
Sequence conflict681E → EE AA sequence Ref.9
Sequence conflict7591Q → H in ABD74692. Ref.3

Secondary structure

............................................................. 911
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02730 [UniParc].

Last modified April 1, 1990. Version 3.
Checksum: 35EC3EE7AFF27D2F

FASTA911101,792
        10         20         30         40         50         60 
MEELQDDYED MMEENLEQEE YEDPDIPESQ MEEPAAHDTE ATATDYHTTS HPGTHKVYVE 

        70         80         90        100        110        120 
LQELVMDEKN QELRWMEAAR WVQLEENLGE NGAWGRPHLS HLTFWSLLEL RRVFTKGTVL 

       130        140        150        160        170        180 
LDLQETSLAG VANQLLDRFI FEDQIRPQDR EELLRALLLK HSHAGELEAL GGVKPAVLTR 

       190        200        210        220        230        240 
SGDPSQPLLP QHSSLETQLF CEQGDGGTEG HSPSGILEKI PPDSEATLVL VGRADFLEQP 

       250        260        270        280        290        300 
VLGFVRLQEA AELEAVELPV PIRFLFVLLG PEAPHIDYTQ LGRAAATLMS ERVFRIDAYM 

       310        320        330        340        350        360 
AQSRGELLHS LEGFLDCSLV LPPTDAPSEQ ALLSLVPVQR ELLRRRYQSS PAKPDSSFYK 

       370        380        390        400        410        420 
GLDLNGGPDD PLQQTGQLFG GLVRDIRRRY PYYLSDITDA FSPQVLAAVI FIYFAALSPA 

       430        440        450        460        470        480 
ITFGGLLGEK TRNQMGVSEL LISTAVQGIL FALLGAQPLL VVGFSGPLLV FEEAFFSFCE 

       490        500        510        520        530        540 
TNGLEYIVGR VWIGFWLILL VVLVVAFEGS FLVRFISRYT QEIFSFLISL IFIYETFSKL 

       550        560        570        580        590        600 
IKIFQDHPLQ KTYNYNVLMV PKPQGPLPNT ALLSLVLMAG TFFFAMMLRK FKNSSYFPGK 

       610        620        630        640        650        660 
LRRVIGDFGV PISILIMVLV DFFIQDTYTQ KLSVPDGFKV SNSSARGWVI HPLGLRSEFP 

       670        680        690        700        710        720 
IWMMFASALP ALLVFILIFL ESQITTLIVS KPERKMVKGS GFHLDLLLVV GMGGVAALFG 

       730        740        750        760        770        780 
MPWLSATTVR SVTHANALTV MGKASTPGAA AQIQEVKEQR ISGLLVAVLV GLSILMEPIL 

       790        800        810        820        830        840 
SRIPLAVLFG IFLYMGVTSL SGIQLFDRIL LLFKPPKYHP DVPYVKRVKT WRMHLFTGIQ 

       850        860        870        880        890        900 
IICLAVLWVV KSTPASLALP FVLILTVPLR RVLLPLIFRN VELQCLDADD AKATFDEEEG 

       910 
RDEYDEVAMP V 

« Hide

References

« Hide 'large scale' references
[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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Phosphorylation sites in human erythrocyte band 3 protein."
Yannoukakos D., Vasseur C., Piau J.-P., Wajcman H., Bursaux E.
Biochim. Biophys. Acta 1061:253-266(1991) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Basis of unique red cell membrane properties in hereditary ovalocytosis."
Schofield A.E., Tanner M.J.A., Pinder J.C., Clough B., Bayley P.M., Nash G.B., Dluzewski A.R., Reardon D.M., Cox T.M., Wilson R.J.M., Gratzer W.B.
J. Mol. Biol. 223:949-958(1992) [PubMed] [Europe PMC] [Abstract]
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]"Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis."
Eber S.W., Gonzalez J.M., Lux M.L., Scarpa A.L., Tse W.T., Dornwell M., Herbers J., Kugler W., Oezcan R., Pekrun A., Gallagher P.G., Schroeter W., Forget B.G., Lux S.E.
Nat. Genet. 13:214-218(1996) [PubMed] [Europe PMC] [Abstract]
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]Erratum
Dhermy D., Galand C., Bournier O., Boulanger L., Cynober T., Schismanoff P.O., Bursaux E., Tchernia G., Boivin P., Garbarz M.
Br. J. Haematol. 99:474-474(1997)
[48]"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.
[49]"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).
[50]"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.
[51]"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.
[52]"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.
[53]"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.
[54]"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.
[55]"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.
[56]"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.
[57]"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.
[58]"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.
[59]"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.
[60]"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.
[61]"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.
[62]"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.
[63]"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.
[64]"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.
[65]"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.
[66]"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.
[67]"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.
[68]"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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS11481.1.
PIRB3HU. A36218.
RefSeqNP_000333.1. NM_000342.3.
XP_005257649.1. XM_005257592.2.
UniGeneHs.443948.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP02730.
SMRP02730. Positions 55-356, 389-430, 803-835.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112412. 11 interactions.
IntActP02730. 2 interactions.
MINTMINT-1344291.
STRING9606.ENSP00000262418.

Protein family/group databases

TCDB2.A.31.1.1. the anion exchanger (ae) family.

PTM databases

PhosphoSiteP02730.

Polymorphism databases

DMDM114787.

Proteomic databases

PaxDbP02730.
PRIDEP02730.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262418; ENSP00000262418; ENSG00000004939.
GeneID6521.
KEGGhsa:6521.
UCSCuc002igf.4. human.

Organism-specific databases

CTD6521.
GeneCardsGC17M042337.
HGNCHGNC:11027. SLC4A1.
HPAHPA015584.
MIM109270. gene+phenotype.
110500. phenotype.
112010. phenotype.
112050. phenotype.
130600. phenotype.
179800. phenotype.
601550. phenotype.
601551. phenotype.
611162. phenotype.
611590. phenotype.
612653. phenotype.
neXtProtNX_P02730.
Orphanet93608. Autosomal dominant distal renal tubular acidosis.
93610. Distal renal tubular acidosis with anemia.
822. Hereditary spherocytosis.
98868. Southeast Asian ovalocytosis.
PharmGKBPA35895.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG268067.
HOVERGENHBG004326.
InParanoidP02730.
KOK06573.
OMAEYDEVAM.
OrthoDBEOG7TMZR0.
PhylomeDBP02730.
TreeFamTF313630.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

BgeeP02730.
GenevestigatorP02730.

Family and domain databases

Gene3D3.40.1100.10. 1 hit.
InterProIPR001717. 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]
PANTHERPTHR11453. PTHR11453. 1 hit.
PfamPF07565. Band_3_cyto. 1 hit.
PF00955. HCO3_cotransp. 2 hits.
[Graphical view]
PRINTSPR00165. ANIONEXCHNGR.
PR01187. ANIONEXHNGR1.
PR01231. HCO3TRNSPORT.
SUPFAMSSF55804. SSF55804. 1 hit.
TIGRFAMsTIGR00834. ae. 1 hit.
PROSITEPS00219. ANION_EXCHANGER_1. 1 hit.
PS00220. ANION_EXCHANGER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02730.
GeneWikiBand_3.
GenomeRNAi6521.
NextBio25367.
PMAP-CutDBP02730.
PROP02730.
SOURCESearch...

Entry information

Entry nameB3AT_HUMAN
AccessionPrimary (citable) accession number: P02730
Secondary accession number(s): G4V2I6 expand/collapse secondary AC list , P78487, Q1ZZ45, Q4KKW9, Q4VB84, Q9UCY7, Q9UDJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 196 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries

Blood group antigen proteins

Nomenclature of blood group antigens and list of entries