Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P02730

- B3AT_HUMAN

UniProt

P02730 - B3AT_HUMAN

(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)

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

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 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 transport Source: UniProtKB
  5. ion transport Source: Reactome
  6. small molecule metabolic process Source: Reactome
  7. transmembrane transport Source: Reactome
Complete GO annotation...

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
Complete GO annotation...

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.
ExpressionAtlasiP02730. baseline and differential.
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.
GeneTreeiENSGT00760000119021.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEELQDDYED MMEENLEQEE YEDPDIPESQ MEEPAAHDTE ATATDYHTTS
60 70 80 90 100
HPGTHKVYVE LQELVMDEKN QELRWMEAAR WVQLEENLGE NGAWGRPHLS
110 120 130 140 150
HLTFWSLLEL RRVFTKGTVL LDLQETSLAG VANQLLDRFI FEDQIRPQDR
160 170 180 190 200
EELLRALLLK HSHAGELEAL GGVKPAVLTR SGDPSQPLLP QHSSLETQLF
210 220 230 240 250
CEQGDGGTEG HSPSGILEKI PPDSEATLVL VGRADFLEQP VLGFVRLQEA
260 270 280 290 300
AELEAVELPV PIRFLFVLLG PEAPHIDYTQ LGRAAATLMS ERVFRIDAYM
310 320 330 340 350
AQSRGELLHS LEGFLDCSLV LPPTDAPSEQ ALLSLVPVQR ELLRRRYQSS
360 370 380 390 400
PAKPDSSFYK GLDLNGGPDD PLQQTGQLFG GLVRDIRRRY PYYLSDITDA
410 420 430 440 450
FSPQVLAAVI FIYFAALSPA ITFGGLLGEK TRNQMGVSEL LISTAVQGIL
460 470 480 490 500
FALLGAQPLL VVGFSGPLLV FEEAFFSFCE TNGLEYIVGR VWIGFWLILL
510 520 530 540 550
VVLVVAFEGS FLVRFISRYT QEIFSFLISL IFIYETFSKL IKIFQDHPLQ
560 570 580 590 600
KTYNYNVLMV PKPQGPLPNT ALLSLVLMAG TFFFAMMLRK FKNSSYFPGK
610 620 630 640 650
LRRVIGDFGV PISILIMVLV DFFIQDTYTQ KLSVPDGFKV SNSSARGWVI
660 670 680 690 700
HPLGLRSEFP IWMMFASALP ALLVFILIFL ESQITTLIVS KPERKMVKGS
710 720 730 740 750
GFHLDLLLVV GMGGVAALFG MPWLSATTVR SVTHANALTV MGKASTPGAA
760 770 780 790 800
AQIQEVKEQR ISGLLVAVLV GLSILMEPIL SRIPLAVLFG IFLYMGVTSL
810 820 830 840 850
SGIQLFDRIL LLFKPPKYHP DVPYVKRVKT WRMHLFTGIQ IICLAVLWVV
860 870 880 890 900
KSTPASLALP FVLILTVPLR RVLLPLIFRN VELQCLDADD AKATFDEEEG
910
RDEYDEVAMP V
Length:911
Mass (Da):101,792
Last modified:April 1, 1990 - v3
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.
GeneTreei ENSGT00760000119021.
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.
ExpressionAtlasi P02730. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 199 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