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P04920 (B3A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Anion exchange protein 2

Short name=AE 2
Short name=Anion exchanger 2
Alternative name(s):
Non-erythroid band 3-like protein
Short name=BND3L
Solute carrier family 4 member 2
Gene names
Name:SLC4A2
Synonyms:AE2, EPB3L1, HKB3, MPB3L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1241 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plasma membrane anion exchange protein of wide distribution.

Subcellular location

Membrane; Multi-pass membrane protein.

Sequence similarities

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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform A (identifier: P04920-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B1 (identifier: P04920-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: MSSAPRRPAKGADSFCT → MTQ
Isoform 3 (identifier: P04920-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: MSSAPRRPAKGADSFCT → MDFLLRPQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12411241Anion exchange protein 2
PRO_0000079215

Regions

Topological domain1 – 707707Cytoplasmic Potential
Transmembrane708 – 73124Helical; Potential
Transmembrane737 – 77438Helical; Potential
Transmembrane784 – 81633Helical; Potential
Transmembrane826 – 84722Helical; Potential
Topological domain848 – 90053Extracellular Potential
Transmembrane901 – 91818Helical; Potential
Topological domain919 – 93315Cytoplasmic Potential
Transmembrane934 – 95421Helical; Potential
Transmembrane988 – 101023Helical; Potential
Transmembrane1036 – 105924Helical; Potential
Transmembrane1091 – 113646Helical; Potential
Transmembrane1163 – 119937Helical; Potential
Region708 – 1241534Membrane (anion exchange)
Compositional bias5 – 320316Pro-rich

Amino acid modifications

Modified residue1131Phosphoserine Ref.9
Modified residue1321Phosphoserine Ref.9
Modified residue1441Phosphoserine Ref.11
Modified residue1701Phosphoserine By similarity
Modified residue1721Phosphoserine By similarity
Modified residue1731Phosphoserine Ref.9
Modified residue1831Phosphothreonine Ref.9
Modified residue2571Phosphothreonine By similarity
Modified residue4431Phosphoserine Ref.13
Lipidation11731S-palmitoyl cysteine By similarity
Glycosylation8591N-linked (GlcNAc...) Potential
Glycosylation8681N-linked (GlcNAc...) Potential
Glycosylation8821N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 1717MSSAP…DSFCT → MDFLLRPQ in isoform 3.
VSP_045953
Alternative sequence1 – 1717MSSAP…DSFCT → MTQ in isoform B1.
VSP_000456
Natural variant261G → E. Ref.2
Corresponds to variant rs2303929 [ dbSNP | Ensembl ].
VAR_025168
Natural variant2021E → V. Ref.2
Corresponds to variant rs2229551 [ dbSNP | Ensembl ].
VAR_025169
Natural variant2081S → T.
Corresponds to variant rs2229552 [ dbSNP | Ensembl ].
VAR_048349
Natural variant3111R → W. Ref.2
Corresponds to variant rs35016052 [ dbSNP | Ensembl ].
VAR_025170
Natural variant12041L → F. Ref.2
Corresponds to variant rs34918764 [ dbSNP | Ensembl ].
VAR_025171

Experimental info

Sequence conflict71R → L in CAA44067. Ref.1
Sequence conflict681E → M in CAA44067. Ref.1
Sequence conflict741H → R in CAA44067. Ref.1
Sequence conflict921D → G in CAA44067. Ref.1
Sequence conflict1221E → V in CAA44067. Ref.1
Sequence conflict1571Q → R in CAA44067. Ref.1
Sequence conflict2481E → R in CAA44067. Ref.1
Sequence conflict3991Missing in CAA27556. Ref.7
Sequence conflict4471L → V in CAA44067. Ref.1
Sequence conflict450 – 47526LLGHH…GGVPE → CWGITMVRGLRVTPTSPSLS WEVFLR in CAA27556. Ref.7
Sequence conflict485 – 4862EL → DV in CAA44067. Ref.1
Sequence conflict485 – 4862EL → DV in CAA27556. Ref.7
Sequence conflict5711E → K in BAG58592. Ref.3
Sequence conflict666 – 68116AAGAA…RTGRP → RQGQLKMIPSADGAA in CAA44067. Ref.1
Sequence conflict666 – 68116AAGAA…RTGRP → RQGQLKMIPSADGAA in CAA27556. Ref.7
Sequence conflict8241Q → R in CAA44067. Ref.1
Sequence conflict8241Q → R in CAA27556. Ref.7
Sequence conflict9021L → P in CAA44067. Ref.1
Sequence conflict9021L → P in CAA27556. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified January 24, 2006. Version 4.
Checksum: 35E32D9FC34DFB61

FASTA1,241137,009
        10         20         30         40         50         60 
MSSAPRRPAK GADSFCTPEP ESLGPGTPGF PEQEEDELHR TLGVERFEEI LQEAGSRGGE 

        70         80         90        100        110        120 
EPGRSYGEED FEYHRQSSHH IHHPLSTHLP PDARRRKTPQ GPGRKPRRRP GASPTGETPT 

       130        140        150        160        170        180 
IEEGEEDEDE ASEAEGARAL TQPSPVSTPS SVQFFLQEDD SADRKAERTS PSSPAPLPHQ 

       190        200        210        220        230        240 
EATPRASKGA QAGTQVEEAE AEAVAVASGT AGGDDGGASG RPLPKAQPGH RSYNLQERRR 

       250        260        270        280        290        300 
IGSMTGAEQA LLPRVPTDEI EAQTLATADL DLMKSHRFED VPGVRRHLVR KNAKGSTQSG 

       310        320        330        340        350        360 
REGREPGPTP RARPRAPHKP HEVFVELNEL LLDKNQEPQW RETARWIKFE EDVEEETERW 

       370        380        390        400        410        420 
GKPHVASLSF RSLLELRRTL AHGAVLLDLD QQTLPGVAHQ VVEQMVISDQ IKAEDRANVL 

       430        440        450        460        470        480 
RALLLKHSHP SDEKDFSFPR NISAGSLGSL LGHHHGQGAE SDPHVTEPLM GGVPETRLEV 

       490        500        510        520        530        540 
ERERELPPPA PPAGITRSKS KHELKLLEKI PENAEATVVL VGCVEFLSRP TMAFVRLREA 

       550        560        570        580        590        600 
VELDAVLEVP VPVRFLFLLL GPSSANMDYH EIGRSISTLM SDKQFHEAAY LADEREDLLT 

       610        620        630        640        650        660 
AINAFLDCSV VLPPSEVQGE ELLRSVAHFQ RQMLKKREEQ GRLLPTGAGL EPKSAQDKAL 

       670        680        690        700        710        720 
LQMVEAAGAA EDDPLRRTGR PFGGLIRDVR RRYPHYLSDF RDALDPQCLA AVIFIYFAAL 

       730        740        750        760        770        780 
SPAITFGGLL GEKTQDLIGV SELIMSTALQ GVVFCLLGAQ PLLVIGFSGP LLVFEEAFFS 

       790        800        810        820        830        840 
FCSSNHLEYL VGRVWIGFWL VFLALLMVAL EGSFLVRFVS RFTQEIFAFL ISLIFIYETF 

       850        860        870        880        890        900 
YKLVKIFQEH PLHGCSASNS SEVDGGENMT WAGARPTLGP GNRSLAGQSG QGKPRGQPNT 

       910        920        930        940        950        960 
ALLSLVLMAG TFFIAFFLRK FKNSRFFPGR IRRVIGDFGV PIAILIMVLV DYSIEDTYTQ 

       970        980        990       1000       1010       1020 
KLSVPSGFSV TAPEKRGWVI NPLGEKSPFP VWMMVASLLP AILVFILIFM ETQITTLIIS 

      1030       1040       1050       1060       1070       1080 
KKERMLQKGS GFHLDLLLIV AMGGICALFG LPWLAAATVR SVTHANALTV MSKAVAPGDK 

      1090       1100       1110       1120       1130       1140 
PKIQEVKEQR VTGLLVALLV GLSIVIGDLL RQIPLAVLFG IFLYMGVTSL NGIQFYERLH 

      1150       1160       1170       1180       1190       1200 
LLLMPPKHHP DVTYVKKVRT LRMHLFTALQ LLCLALLWAV MSTAASLAFP FILILTVPLR 

      1210       1220       1230       1240 
MVVLTRIFTD REMKCLDANE AEPVFDEREG VDEYNEMPMP V 

« Hide

Isoform B1 [UniParc].

Checksum: BA59FBFDF46178F2
Show »

FASTA1,227135,606
Isoform 3 [UniParc].

Checksum: C57606D7CA9D34D2
Show »

FASTA1,232136,247

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of band 3 related anion transport protein AE2 from human kidney."
Gehrig H., Mueller W., Appelhans H.
Biochim. Biophys. Acta 1130:326-328(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[2]NIEHS SNPs program
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-26; VAL-202; TRP-311 AND PHE-1204.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND 3).
Tissue: Hippocampus.
[4]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM B1).
Tissue: Brain.
[7]"Cloning and structural characterization of a human non-erythroid band 3-like protein."
Demuth D.R., Showe L.C., Ballantine M., Palumbo A., Fraser P.J., Cioe L., Rovera G., Curtis P.J.
EMBO J. 5:1205-1214(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 375-1241.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-132; SER-173 AND THR-183, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X62137 mRNA. Translation: CAA44067.1.
DQ149844 Genomic DNA. Translation: AAZ38724.1.
AK295767 mRNA. Translation: BAG58592.1.
AK312699 mRNA. Translation: BAG35577.1.
AC010973 Genomic DNA. No translation available.
CH471173 Genomic DNA. Translation: EAW54046.1.
CH471173 Genomic DNA. Translation: EAW54047.1.
BC009386 mRNA. Translation: AAH09386.1.
BC009434 mRNA. Translation: AAH09434.1.
X03918 mRNA. Translation: CAA27556.1.
PIRS21086.
RefSeqNP_001186621.1. NM_001199692.1.
NP_001186622.1. NM_001199693.1.
NP_001186623.1. NM_001199694.1.
NP_003031.3. NM_003040.3.
UniGeneHs.647069.

3D structure databases

ProteinModelPortalP04920.
SMRP04920. Positions 322-637, 692-733, 1133-1165.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112413. 2 interactions.
IntActP04920. 4 interactions.
STRING9606.ENSP00000311402.

Protein family/group databases

TCDB2.A.31.1.2. the anion exchanger (ae) family.

PTM databases

PhosphoSiteP04920.

Polymorphism databases

DMDM85687559.

Proteomic databases

PaxDbP04920.
PeptideAtlasP04920.
PRIDEP04920.

Protocols and materials databases

DNASU6522.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000392826; ENSP00000376571; ENSG00000164889. [P04920-3]
ENST00000413384; ENSP00000405600; ENSG00000164889. [P04920-1]
ENST00000461735; ENSP00000419164; ENSG00000164889. [P04920-2]
ENST00000485713; ENSP00000419412; ENSG00000164889. [P04920-1]
GeneID6522.
KEGGhsa:6522.
UCSCuc003wit.4. human. [P04920-1]
uc003wiu.4. human. [P04920-2]

Organism-specific databases

CTD6522.
GeneCardsGC07P150754.
HGNCHGNC:11028. SLC4A2.
HPAHPA019339.
MIM109280. gene.
neXtProtNX_P04920.
PharmGKBPA35896.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG268067.
HOVERGENHBG004326.
InParanoidP04920.
KOK13855.
OMAGADSFCT.
OrthoDBEOG7TMZR0.
PhylomeDBP04920.
TreeFamTF313630.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP04920.
BgeeP04920.
CleanExHS_SLC4A2.
GenevestigatorP04920.

Family and domain databases

Gene3D3.40.1100.10. 1 hit.
InterProIPR001717. Anion_exchange.
IPR002978. Anion_exchange_2.
IPR018241. Anion_exchange_CS.
IPR013769. Band3_cytoplasmic_dom.
IPR011531. HCO3_transpt_C.
IPR003020. HCO3_transpt_euk.
IPR016152. PTrfase/Anion_transptr.
[Graphical view]
PANTHERPTHR11453. PTHR11453. 1 hit.
PTHR11453:SF14. PTHR11453:SF14. 1 hit.
PfamPF07565. Band_3_cyto. 1 hit.
PF00955. HCO3_cotransp. 1 hit.
[Graphical view]
PRINTSPR00165. ANIONEXCHNGR.
PR01188. ANIONEXHNGR2.
PR01231. HCO3TRNSPORT.
SUPFAMSSF55804. SSF55804. 2 hits.
TIGRFAMsTIGR00834. ae. 1 hit.
PROSITEPS00219. ANION_EXCHANGER_1. 1 hit.
PS00220. ANION_EXCHANGER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSLC4A2. human.
GeneWikiSLC4A2.
GenomeRNAi6522.
NextBio25371.
PROP04920.
SOURCESearch...

Entry information

Entry nameB3A2_HUMAN
AccessionPrimary (citable) accession number: P04920
Secondary accession number(s): B2R6T0 expand/collapse secondary AC list , B4DIT0, D3DX05, F8W682, Q45EY5, Q969L3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 24, 2006
Last modified: April 16, 2014
This is version 154 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM