P02730 (B3AT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SLC4A1
Synonyms:	AE1, DI, EPB3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	911 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Band 3 is the major integral glycoprotein of the erythrocyte membrane. Band 3 has two functional domains. Its integral domain mediates a 1:1 exchange of inorganic anions across the membrane, whereas its cytoplasmic domain provides binding sites for cytoskeletal proteins, glycolytic enzymes, and hemoglobin.
Enzyme regulation	Phenyl isothiocyanate inhibits anion transport in vitro.
Subunit structure	A dimer in solution, it spans the membrane asymmetrically and appears to be tetrameric. Interacts (via cytoplasmic N-terminus domain) with ANK1 (via N-terminus ANK repeats). Ref.17
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Erythrocytes.
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.15 Ref.18 Phosphorylated on Tyr-359 and Tyr-904 most likely by LYN. PP1-inhibited phosphorylation that follows Tyr-8 and Tyr-21 phosphorylation. Ref.15 Ref.18
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.28 Ref.30 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.13 Ref.29 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.44 Ref.49 Ref.51 Ref.52 Ref.57 Ref.60 Ref.61 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 process	Anion exchange Ion transport Transport
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation Elliptocytosis Hereditary hemolytic anemia
Domain	Transmembrane Transmembrane helix
Molecular function	Blood group antigen
PTM	Acetylation Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	bicarbonate transport Traceable author statement. Source: Reactome cellular ion homeostasis Traceable author statement PubMed 8841202. Source: ProtInc small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	Z disc Inferred from sequence or structural similarity. Source: UniProtKB basolateral plasma membrane Inferred from direct assay PubMed 12539048Ref.59. Source: UniProtKB cortical cytoskeleton Inferred from direct assay PubMed 16669616. Source: UniProtKB integral to plasma membrane Inferred from direct assay PubMed 379653. Source: BHF-UCL
Molecular_function	chloride transmembrane transporter activity Inferred from sequence or structural similarity. Source: UniProtKB inorganic anion exchanger activity Traceable author statement. Source: Reactome protein anchor Traceable author statement PubMed 10950304. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 911

911

Band 3 anion transport protein

PRO_0000079209

Regions

Topological domain

1 – 403

403

Cytoplasmic

Transmembrane

404 – 424

21

Helical; Potential

Transmembrane

437 – 456

20

Helical; Potential

Transmembrane

460 – 479

20

Helical; Potential

Transmembrane

491 – 510

20

Helical; Potential

Transmembrane

523 – 541

19

Helical; Potential

Topological domain

542 – 568

27

Extracellular Potential

Transmembrane

569 – 588

20

Helical; Potential

Topological domain

589 – 603

15

Cytoplasmic Potential

Transmembrane

604 – 624

21

Helical; Potential

Topological domain

625 – 660

36

Extracellular Potential

Transmembrane

661 – 680

20

Helical; Potential

Transmembrane

699 – 719

21

Helical; Potential

Transmembrane

763 – 780

18

Helical; Potential

Transmembrane

785 – 806

22

Helical; Potential

Transmembrane

844 – 865

22

Helical; Potential

Region

404 – 911

508

Membrane (anion exchange)

Region

559 – 630

72

Involved in anion transport

Sites

Site

590

1

Important for anion transport

Site

681

1

Important for anion-proton cotransport

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.8

Modified residue

8

1

Phosphotyrosine Ref.15 Ref.18

Modified residue

21

1

Phosphotyrosine Ref.15 Ref.18

Modified residue

46

1

Phosphotyrosine Ref.15

Modified residue

350

1

Phosphoserine By similarity

Modified residue

359

1

Phosphotyrosine Ref.18

Modified residue

904

1

Phosphotyrosine Ref.18

Lipidation

843

1

S-palmitoyl cysteine Ref.16

Glycosylation

642

1

N-linked (GlcNAc...) Probable

Natural variations

Natural variant

27

1

P → H. Ref.5
Corresponds to variant rs55777403 [ dbSNP | Ensembl ].

VAR_058035

Natural variant

38

1

D → A. Ref.3 Ref.4 Ref.39 Ref.52
Corresponds to variant rs5035 [ dbSNP | Ensembl ].

VAR_014612

Natural variant

40

1

E → K in hemolytic anemia; Montefiore. Ref.32 Ref.37
Corresponds to variant rs45562031 [ dbSNP | Ensembl ].

VAR_000798

Natural variant

45

1

D → E.
Corresponds to variant rs34700496 [ dbSNP | Ensembl ].

VAR_036693

Natural variant

56

1

K → E in Di(a)/Memphis-II antigen. Ref.4 Ref.27 Ref.28 Ref.33 Ref.52
Corresponds to variant rs5036 [ dbSNP | Ensembl ].

VAR_000799

Natural variant

68

1

E → K.
Corresponds to variant rs13306787 [ dbSNP | Ensembl ].

VAR_039290

Natural variant

72

1

E → D. Ref.52

VAR_058036

Natural variant

73

1

L → M. Ref.39

VAR_039291

Natural variant

90

1

E → K in SPH4; Cape Town. Ref.57
Corresponds to variant rs28929480 [ dbSNP | Ensembl ].

VAR_013784

Natural variant

112

1

R → S.
Corresponds to variant rs5037 [ dbSNP | Ensembl ].

VAR_014613

Natural variant

130

1

G → R in SPH4; Fukoka. Ref.52

VAR_013785

Natural variant

147

1

P → S in SPH4; Mondego. Ref.38

VAR_013786

Natural variant

285

1

A → D in SPH4; Boston. Ref.36

VAR_013787

Natural variant

327

1

P → R in SPH4; Tuscaloosa. Ref.29
Corresponds to variant rs28931583 [ dbSNP | Ensembl ].

VAR_000800

Natural variant

400 – 408

9

Missing in EL4.

VAR_000801

Natural variant

429

1

E → D in NFLD+ antigen. Ref.54

VAR_058037

Natural variant

432

1

R → W in ELO antigen.

VAR_013788

Natural variant

442

1

I → F.
Corresponds to variant rs5018 [ dbSNP | Ensembl ].

VAR_014614

Natural variant

455

1

G → E in SPH4; Benesov. Ref.36

VAR_013789

Natural variant

455

1

G → R in SPH4; Yamagata. Ref.52

VAR_058038

Natural variant

480

1

E → K in FR(a+) antigen. Ref.55

VAR_013790

Natural variant

488

1

V → M in SPH4; Coimbra; also in AR-dRTA. Ref.38 Ref.51
Corresponds to variant rs28931584 [ dbSNP | Ensembl ].

VAR_013791

Natural variant

490

1

R → C in SPH4; Bicetre I. Ref.40

VAR_013792

Natural variant

490

1

R → H in SPH4; Pinhal. Ref.49

VAR_058039

Natural variant

508

1

E → K. Ref.4
Corresponds to variant rs45568837 [ dbSNP | Ensembl ].

VAR_025090

Natural variant

518

1

R → C in SPH4; Dresden. Ref.37

VAR_000802

Natural variant

548

1

P → L in RB(A) antigen.

VAR_000803

Natural variant

551

1

K → N in TR(A) antigen.

VAR_013793

Natural variant

552

1

T → I in WARR antigen.

VAR_000804

Natural variant

555

1

Y → H in VG(a) antigen.

VAR_013794

Natural variant

557

1

V → M in WD(a) antigen.

VAR_000805

Natural variant

561

1

P → A in NFLD+ antigen. Ref.54

VAR_058040

Natural variant

561

1

P → S in BOW antigen. Ref.54

VAR_013795

Natural variant

565

1

G → A in WU antigen.

VAR_013796

Natural variant

566

1

P → A in KREP antigen.

VAR_013797

Natural variant

566

1

P → S in PN(a) antigen.

VAR_013798

Natural variant

569

1

N → K in BP(a) antigen.

VAR_013799

Natural variant

586

1

M → L.
Corresponds to variant rs5019 [ dbSNP | Ensembl ].

VAR_014615

Natural variant

589

1

R → C in AD-dRTA; reduced red cell sulfate transport and altered glycosylation of the red cell band 3 N-glycan chain. Ref.42

VAR_015104

Natural variant

589

1

R → H in AD-dRTA. Ref.42 Ref.47

VAR_015105

Natural variant

589

1

R → S in AD-dRTA. Ref.47

VAR_015106

Natural variant

602

1

R → P in dRTA-HA. Ref.58

VAR_039292

Natural variant

609

1

G → 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.59

VAR_058041

Natural variant

613

1

S → F in AD-dRTA; markedly increased red cell sulfate transport but almost normal red cell iodide transport. Ref.42

VAR_015107

Natural variant

646

1

R → Q in SW(a+) antigen. Ref.56

VAR_013800

Natural variant

646

1

R → W in SW(a+) antigen. Ref.56

VAR_013801

Natural variant

656

1

R → C in HG(a) antigen.

VAR_013802

Natural variant

656

1

R → H in MO(a) antigen.

VAR_013803

Natural variant

658

1

E → K in WR(a) antigen. Ref.34

VAR_000806

Natural variant

663

1

M → K in SPH4; Tambau. Ref.60

VAR_058042

Natural variant

663

1

Missing in SPH4; Osnabruck II. Ref.37

VAR_000807

Natural variant

687

1

L → P in SPH4. Ref.61

VAR_039293

Natural variant

688

1

I → V.
Corresponds to variant rs5022 [ dbSNP | Ensembl ].

VAR_014616

Natural variant

690

1

S → G.
Corresponds to variant rs5023 [ dbSNP | Ensembl ].

VAR_014617

Natural variant

701

1

G → D in dRTA-HA. Ref.46 Ref.50

VAR_015171

Natural variant

705

1

D → Y in SPH4. Ref.61

VAR_039294

Natural variant

707

1

L → P in SPH4; Most. Ref.36 Ref.53

VAR_013804

Natural variant

714

1

G → R in SPH4; Okinawa. Ref.52

VAR_013805

Natural variant

731

1

S → P in SPH4. Ref.61

VAR_039295

Natural variant

734

1

H → R in SPH4. Ref.61

VAR_039296

Natural variant

760

1

R → Q in SPH4; Prague II. Ref.35 Ref.52 Ref.53 Ref.61

VAR_013806

Natural variant

760

1

R → W in SPH4; Hradec Kralove. Ref.35 Ref.52 Ref.53

VAR_013807

Natural variant

771

1

G → D in SPH4; Chur. Ref.13

VAR_013808

Natural variant

773

1

S → P in dRTA-NRC. Ref.58

VAR_039297

Natural variant

783

1

I → N in SPH4; Napoli II. Ref.39

VAR_013809

Natural variant

808

1

R → C in SPH4; Jablonec. Ref.35 Ref.53

VAR_013810

Natural variant

808

1

R → H in SPH4; Nara. Ref.52

VAR_013811

Natural variant

832

1

R → H.
Corresponds to variant rs5025 [ dbSNP | Ensembl ].

VAR_014618

Natural variant

834

1

H → P in SPH4; Birmingham. Ref.36 Ref.53

VAR_013812

Natural variant

837

1

T → A in SPH4; Tokyo. Ref.44

VAR_013813

Natural variant

837

1

T → M in SPH4; Philadelphia. Ref.36 Ref.40 Ref.52 Ref.53

VAR_013814

Natural variant

837

1

T → R in SPH4; Nagoya. Ref.52

VAR_058043

Natural variant

850

1

Missing in dRTA-HA. Ref.50

VAR_015109

Natural variant

854

1

P → L in Di(a)/Memphis-II antigen. Ref.33 Ref.52
Corresponds to variant rs2285644 [ dbSNP | Ensembl ].

VAR_000808

Natural variant

858

1

A → D in AD-dRTA. Ref.50

VAR_015108

Natural variant

862

1

V → I. Ref.4
Corresponds to variant rs5026 [ dbSNP | Ensembl ].

VAR_014619

Natural variant

868

1

P → L in acanthocytosis; due to band 3 high transport. Ref.31

VAR_013815

Natural variant

870

1

R → W in SPH4; Prague III. Ref.35 Ref.53 Ref.57
Corresponds to variant rs28931585 [ dbSNP | Ensembl ].

VAR_013816

Experimental info

Sequence conflict

11

1

M → D AA sequence Ref.7

Sequence conflict

68

1

E → EE AA sequence Ref.7

Sequence conflict

759

1

Q → H in ABD74692. Ref.3

Secondary structure

1

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911

Helix Strand Turn

Details...

Beta strand

58 – 67

10

Turn

68 – 70

3

Beta strand

73 – 88

16

Helix

104 – 115

12

Beta strand

118 – 123

6

Helix

128 – 141

14

Helix

147 – 149

3

Helix

150 – 157

8

Helix

164 – 170

7

Beta strand

173 – 175

3

Helix

195 – 200

6

Helix

212 – 219

8

Beta strand

226 – 234

9

Beta strand

241 – 251

11

Beta strand

256 – 258

3

Beta strand

262 – 270

9

Helix

278 – 289

12

Helix

292 – 300

9

Helix

304 – 316

13

Beta strand

319 – 321

3

Helix

328 – 333

6

Helix

335 – 346

12

Turn

392 – 394

3

Helix

395 – 399

5

Helix

409 – 422

14

Helix

437 – 453

17

Turn

806 – 809

4

Helix

829 – 833

5

Sequences

	Sequence		Length	Mass (Da)
	P02730 [UniParc]. Last modified April 1, 1990. Version 3. Checksum: 35EC3EE7AFF27D2F	FASTA	911	101,792
	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

References

	« Hide 'large scale' referencesShow '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]	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.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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].
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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.
[34]	"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.
[35]	"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.
[36]	"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.
[37]	"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.
[38]	"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.
[39]	"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.
[40]	"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.
[41]	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)
[42]	"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.
[43]	"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).
[44]	"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.
[45]	"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.
[46]	"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.
[47]	"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.
[48]	"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.
[49]	"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.
[50]	"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.
[51]	"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.
[52]	"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.
[53]	"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.
[54]	"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.
[55]	"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.
[56]	"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.
[57]	"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.
[58]	"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.
[59]	"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.
[60]	"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.
[61]	"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.
+	Additional computationally mapped references.

Web resources

Wikipedia

Band 3 entry

dbRBC/BGMUT

Blood group antigen gene mutation database

GeneReviews

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X12609 mRNA. Translation: CAA31128.1.
M27819 mRNA. Translation: AAA35514.1.
DQ419529 mRNA. Translation: ABD74692.1.
DQ072115 Genomic DNA. Translation: AAY57324.1.
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.

IPI

IPI00791534.

PIR

B3HU. A36218.

RefSeq

NP_000333.1. NM_000342.3.

UniGene

Hs.443948.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

DisProt

DP00426.

ProteinModelPortal

P02730.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1344291.

STRING

9606.ENSP00000262418.

Protein family/group databases

TCDB

2.A.31.1.1. anion exchanger (AE) family.

PTM databases

PhosphoSite

P02730.

Polymorphism databases

DMDM

114787.

Proteomic databases

PaxDb

P02730.

PRIDE

P02730.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000262418; ENSP00000262418; ENSG00000004939.

GeneID

6521.

KEGG

hsa:6521.

UCSC

uc002igf.4. human.

Organism-specific databases

CTD

6521.

GeneCards

GC17M042337.

HGNC

HGNC:11027. SLC4A1.

HPA

HPA015584.

MIM

109270. gene+phenotype.
110500. phenotype.
112010. phenotype.
112050. phenotype.
130600. phenotype.
179800. phenotype.
601550. phenotype.
601551. phenotype.
611162. phenotype.
611590. phenotype.
612653. phenotype.

neXtProt

NX_P02730.

Orphanet

18. Distal renal tubular acidosis.
288. Hereditary elliptocytosis.
822. Hereditary spherocytosis.

PharmGKB

PA35895.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG268067.

HOVERGEN

HBG004326.

InParanoid

P02730.

KO

K06573.

OMA

WSLLELQ.

OrthoDB

EOG4W0XCF.

PhylomeDB

P02730.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpress

P02730.

Bgee

P02730.

Genevestigator

P02730.

GermOnline

ENSG00000004939. Homo sapiens.

Family and domain databases

Gene3D

3.40.1100.10. 1 hit.

InterPro

IPR001717. Anion_exchange.
IPR002977. Anion_exchange_1.
IPR018241. Anion_exchange_CS.
IPR013769. Band3_cytoplasmic_dom.
IPR011531. HCO3_transpt_C.
IPR003020. HCO3_transpt_euk.
IPR016152. PTrfase/Anion_transptr.
[Graphical view]

PANTHER

PTHR11453. PTHR11453. 1 hit.

Pfam

PF07565. Band_3_cyto. 1 hit.
PF00955. HCO3_cotransp. 2 hits.
[Graphical view]

PRINTS

PR00165. ANIONEXCHNGR.
PR01187. ANIONEXHNGR1.
PR01231. HCO3TRNSPORT.

SUPFAM

SSF55804. PTrfase/Anion_transptr. 1 hit.

TIGRFAMs

TIGR00834. ae. 1 hit.

PROSITE

PS00219. ANION_EXCHANGER_1. 1 hit.
PS00220. ANION_EXCHANGER_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P02730.

GenomeRNAi

6521.

NextBio

25367.

PMAP-CutDB

P02730.

SOURCE

Search...

Entry information

Entry name

B3AT_HUMAN

Accession

Primary (citable) accession number: P02730
Secondary accession number(s): P78487 , Q1ZZ45, Q4KKW9, Q4VB84, Q9UCY7, Q9UDJ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 1, 1990
Last modified:	May 1, 2013
This is version 182 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.