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P02724 (GLPA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. Feed History...

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

Names and origin

Protein namesRecommended name:
Glycophorin-A
Alternative name(s):
MN sialoglycoprotein
PAS-2
Sialoglycoprotein alpha
CD_antigen=CD235a
Gene names
Name:GYPA
Synonyms:GPA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length150 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). Ref.21 Ref.23 Ref.26 Ref.29 Ref.30 Ref.32

Subunit structure

Homodimer. Interacts with Streptococcus gordonii hsa protein. Ref.19 Ref.24 Ref.31

Subcellular location

Cell membrane; Single-pass type I membrane protein. Note: Appears to be colocalized with SLC4A1. Ref.25

Post-translational modification

The major O-linked glycan are NeuAc-alpha-(2-3)-Gal-beta-(1-3)-[NeuAc-alpha-2-6]-GalNAcOH (about 78 %) and NeuAc-alpha-(2-3)-Gal-beta-(1-3)-GalNAcOH (17 %). Minor O-glycans (5 %) include NeuAc-alpha-(2-3)-Gal-beta-(1-3)-[NeuAc-alpha-2-6]-GalNAcOH NeuAc-alpha-(2-8)-NeuAc-alpha-(2-3)-Gal-beta-(1-3)-GalNAcOH. About 1% of all O-linked glycans carry blood group A, B and H determinants. They derive from a type-2 precursor core structure, Gal-beta-(1,3)-GlcNAc-beta-1-R, and the antigens are synthesized by addition of fucose (H antigen-specific) and then N-acetylgalactosamine (A antigen-specific) or galactose (B antigen-specific). Specifically O-linked-glycans are NeuAc-alpha-(2-3)-Gal-beta-(1-3)-GalNAcOH-(6-1)-GlcNAc-beta-(4-1)-[Fuc-alpha-1-2]-Gal-beta-(3-1)-GalNAc-alpha (about 1%, B antigen-specific) and NeuAc-alpha-(2-3)-Gal-beta-(1-3)-GalNAcOH-(6-1)-GlcNAc-beta-(4-1)-[Fuc-alpha-1-2]-Gal-beta (1 %, O antigen-, A antigen- and B antigen-specific).

Polymorphism

Along with GYPB, GYPA is responsible for the MNS blood group system. The molecular basis of the GPA M/N bloodgroup antigen is a variation at positions 20 and 24. Ser-20 and Gly-24 correspond to M (shown); 'Leu-20' and 'Glu-24' correspond to N.

GYPA polymorphisms are involved in resistance to malaria [MIM:611162].

Miscellaneous

Involved in several unequal homologous recombinations or gene conversion events, predominantly with GYPB and more rarely with GYPE. The resulting fusion proteins are observed in different phenotypes and encode low incidence bloodgroup antigens.

Sequence similarities

Belongs to the glycophorin A family.

Sequence caution

The sequence AAA52624.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-702665,EBI-702665

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P02724-1)

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 2 (identifier: P02724-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.
Isoform 3 (identifier: P02724-3)

The sequence of this isoform differs from the canonical sequence as follows:
     13-45: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.11
Chain20 – 150131Glycophorin-A
PRO_0000012134

Regions

Topological domain20 – 9172Extracellular
Transmembrane92 – 11423Helical
Topological domain115 – 15036Cytoplasmic

Amino acid modifications

Glycosylation211O-linked (GalNAc...) Ref.11 Ref.20
Glycosylation221O-linked (GalNAc...) Ref.11 Ref.20
Glycosylation231O-linked (GalNAc...) Ref.11 Ref.20
Glycosylation291O-linked (GalNAc...) Ref.11 Ref.20
Glycosylation301O-linked (GalNAc...) Ref.11 Ref.20
Glycosylation311O-linked (GalNAc...) Ref.11 Ref.20
Glycosylation321O-linked (GalNAc...) Ref.11 Ref.20
Glycosylation361O-linked (GalNAc...) Ref.20
Glycosylation381O-linked (GalNAc...) Ref.20
Glycosylation411O-linked (GalNAc...) Ref.11 Ref.20
Glycosylation441O-linked (GalNAc...) Ref.11 Ref.20
Glycosylation451N-linked (GlcNAc...) Ref.11 Ref.20
Glycosylation521O-linked (GalNAc...) Ref.20
Glycosylation561O-linked (GalNAc...) Ref.11 Ref.20
Glycosylation631O-linked (GalNAc...) Ref.11 Ref.20
Glycosylation661O-linked (GalNAc...) Ref.11 Ref.20
Glycosylation691O-linked (GalNAc...) Ref.11 Ref.20

Natural variations

Alternative sequence1 – 2626Missing in isoform 2.
VSP_047822
Alternative sequence13 – 4533Missing in isoform 3.
VSP_047823
Natural variant131E → A. Ref.1 Ref.3 Ref.4 Ref.5 Ref.7 Ref.9 Ref.10
Corresponds to variant rs4449373 [ dbSNP | Ensembl ].
VAR_058911
Natural variant131E → G.
Corresponds to variant rs4449373 [ dbSNP | Ensembl ].
VAR_059977
Natural variant201S → L in N antigen and M(g) antigen. Ref.2 Ref.8 Ref.9
Corresponds to variant rs7682260 [ dbSNP | Ensembl ].
VAR_003190
Natural variant231T → N in M(g) antigen. Ref.15
VAR_058912
Natural variant241G → D.
Corresponds to variant rs7658293 [ dbSNP | Ensembl ].
VAR_058913
Natural variant241G → E in N antigen, in M(c) antigen and in M(g) antigen. Ref.2 Ref.8 Ref.9 Ref.14
Corresponds to variant rs7687256 [ dbSNP | Ensembl ].
VAR_003191
Natural variant461D → E in Ny(a) antigen. Ref.40
VAR_058914
Natural variant471T → K in ENEH/Hut antigen. Ref.37
VAR_058915
Natural variant471T → M in ENEH/Vw antigen. Ref.36
VAR_058916
Natural variant501R → W in Or antigen.
VAR_058917
Natural variant661S → Y in Vr antigen. Ref.41
Corresponds to variant rs56077914 [ dbSNP | Ensembl ].
VAR_058918
Natural variant731P → S in Os(a) antigen. Ref.40
VAR_058919
Natural variant761E → K in Ri(a) antigen.
VAR_058920
Natural variant771T → I in Mt(a) antigen. Ref.41
Corresponds to variant rs56172553 [ dbSNP | Ensembl ].
VAR_058921
Natural variant781G → R in ERIK antigen. Ref.38
Corresponds to variant rs1800582 [ dbSNP | Ensembl ].
VAR_058922
Natural variant821Q → K in ENAV/MARS antigen.
VAR_058923
Natural variant841A → P in ENEP/HAG antigen. Ref.39
VAR_058924

Experimental info

Mutagenesis871F → C: Diminishes dimerization. Ref.26
Mutagenesis881S → C: Diminishes dimerization. Ref.26
Mutagenesis901P → C: Diminishes dimerization. Ref.26
Mutagenesis911E → C: Diminishes dimerization. Ref.26
Mutagenesis941L → I: Diminishes dimerization. Ref.23
Mutagenesis951I → A: Diminishes dimerization. Ref.23
Mutagenesis981G → L: Diminishes dimerization. Ref.23
Mutagenesis1021G → L: Abolishes dimerization. Ref.23
Sequence conflict301S → T AA sequence Ref.11
Sequence conflict361T → S AA sequence Ref.11
Sequence conflict1331T → R in AAA88044. Ref.1

Secondary structure

..... 150
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 22, 2009. Version 2.
Checksum: 48A5450E22FA99C9

FASTA15016,331
        10         20         30         40         50         60 
MYGKIIFVLL LSEIVSISAS STTGVAMHTS TSSSVTKSYI SSQTNDTHKR DTYAATPRAH 

        70         80         90        100        110        120 
EVSEISVRTV YPPEEETGER VQLAHHFSEP EITLIIFGVM AGVIGTILLI SYGIRRLIKK 

       130        140        150 
SPSDVKPLPS PDTDVPLSSV EIENPETSDQ 

« Hide

Isoform 2 [UniParc].

Checksum: D257CA020BB42AFD
Show »

FASTA12413,649
Isoform 3 [UniParc].

Checksum: 3F1878ED9D7ADB29
Show »

FASTA11713,000

References

« Hide 'large scale' references
[1]"Isolation and characterization of human glycophorin A cDNA clones by a synthetic oligonucleotide approach: nucleotide sequence and mRNA structure."
Siebert P.D., Fukuda M.
Proc. Natl. Acad. Sci. U.S.A. 83:1665-1669(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-13.
[2]"Isolation of cDNA clones for human erythrocyte membrane sialoglycoproteins alpha and delta."
Tate C.G., Tanner M.J.A.
Biochem. J. 254:743-750(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS N LEU-20 AND GLU-24.
[3]"Structural organization of glycophorin A and B genes: glycophorin B gene evolved by homologous recombination at Alu repeat sequences."
Kudo S., Fukuda M.
Proc. Natl. Acad. Sci. U.S.A. 86:4619-4623(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-13.
[4]"The mechanism of production of multiple mRNAs for human glycophorin A."
Jawad K., Burness T.H.
Nucleic Acids Res. 18:5829-5836(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-13.
Tissue: Blood.
[5]"Characterization of glycophorin A transcripts: control by the common erythroid-specific promoter and alternative usage of different polyadenylation signals."
Kudo S., Onda M., Fukuda M.
J. Biochem. 116:183-192(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-13.
Tissue: Blood.
[6]"Extensive alternative splicing of glycophorins in Southeast Asian populations."
Hsu K., Huang S.-Y., Chi N., Lin M.
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
Tissue: Blood.
[7]"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] (ISOFORM 1), VARIANT ALA-13.
Tissue: Kidney.
[8]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS N LEU-20 AND GLU-24.
[9]"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 1), VARIANT ALA-13, VARIANTS N LEU-20 AND GLU-24.
Tissue: Bone marrow and Lung.
[10]"Molecular biological study of the structure and expression of human glycophorin A."
Siebert P.D., Fukuda M.
Rev. Fr. Transfus. Immunohematol. 29:251-266(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-145 (ISOFORM 1), VARIANT ALA-13.
[11]"Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin."
Tomita M., Marchesi V.T.
Proc. Natl. Acad. Sci. U.S.A. 72:2964-2968(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-150.
[12]Furthmayr H., Galardy R., Tomita M., Marchesi V.T.
Submitted (JUN-1977) to the PIR data bank
Cited for: SEQUENCE REVISION TO 81-120.
[13]"Characterization of cDNA clones for human glycophorin A. Use for gene localization and for analysis of normal of glycophorin-A-deficient (Finnish type) genomic DNA."
Rahuel C., London J., D'Auriol L., Mattei M.-G., Tournamille C., Skrzynia C., Lebouc Y., Galibert F., Cartron J.-P.
Eur. J. Biochem. 172:147-153(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-150.
[14]"Mg and Mc: mutations within the amino-terminal region of glycophorin A."
Furthmayr H., Metaxas M.N., Metaxas-Buhler M.
Proc. Natl. Acad. Sci. U.S.A. 78:631-635(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, VARIANT M(C) GLU-24.
[15]"Amino acid and carbohydrate structural variants of glycoprotein products (M-N glycoproteins) of the M-N allelic locus."
Blumenfeld O.O., Adamany A.M., Puglia K.V.
Proc. Natl. Acad. Sci. U.S.A. 78:747-751(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, VARIANT M(G) ASN-23.
[16]"Structural studies on human erythrocyte glycoproteins. Alkali-labile oligosaccharides."
Thomas D.B., Winzler R.J.
J. Biol. Chem. 244:5943-5946(1969) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION.
[17]"Erythrocytes deficiency in glycophorin resist invasion by the malarial parasite Plasmodium falciparum."
Pasvol G., Wainscoat J.S., Weatherall D.J.
Nature 297:64-66(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMORPHISM, INVOLVEMENT IN RESISTANCE TO MALARIA.
[18]"Structures of novel sialylated O-linked oligosaccharides isolated from human erythrocyte glycophorins."
Fukuda M., Lauffenburger M., Sasaki H., Rogers M.E., Dell A.
J. Biol. Chem. 262:11952-11957(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION.
[19]"The glycophorin A transmembrane domain dimer: sequence-specific propensity for a right-handed supercoil of helices."
Treutlein H.R., Lemmon M.A., Engelman D.M., Brunger A.T.
Biochemistry 31:12726-12732(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[20]"Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A."
Pisano A., Redmond J.W., Williams K.L., Gooley A.A.
Glycobiology 3:429-435(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-21; THR-22; THR-23; THR-29; SER-30; THR-31; SER-32; THR-36; SER-38; SER-41; THR-44; ASN-45; THR-52; THR-56; SER-63; SER-66 AND THR-69, PARTIAL PROTEIN SEQUENCE.
[21]"Receptor and ligand domains for invasion of erythrocytes by Plasmodium falciparum."
Sim B.K., Chitnis C.E., Wasniowska K., Hadley T.J., Miller L.H.
Science 264:1941-1944(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS RECEPTOR FOR PLASMODIUM EBA-175.
[22]"Identification of blood group A and B antigens in human glycophorin."
Podbielska M., Krotkiewski H.
Arch. Immunol. Ther. Exp. 48:211-221(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION (AB BLOOD GROUP ANTIGENS).
[23]"Red-cell glycophorin A-band 3 interactions associated with the movement of band 3 to the cell surface."
Young M.T., Beckmann R., Toye A.M., Tanner M.J.
Biochem. J. 350:53-60(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LEU-94; ILE-95; GLY-98 AND GLY-102.
[24]"Glycophorin A dimerization and band 3 interaction during erythroid membrane biogenesis: in vivo studies in human glycophorin A transgenic mice."
Auffray I., Marfatia S., de Jong K., Lee G., Huang C.H., Paszty C., Tanner M.J., Mohandas N., Chasis J.A.
Blood 97:2872-2878(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[25]"In vivo detection of hetero-association of glycophorin-A and its mutants within the membrane."
Gerber D., Shai Y.
J. Biol. Chem. 276:31229-31232(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[26]"Distinct regions of human glycophorin A enhance human red cell anion exchanger (band 3; AE1) transport function and surface trafficking."
Young M.T., Tanner M.J.
J. Biol. Chem. 278:32954-32961(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF PHE-87; SER-88; PRO-90 AND GLU-91.
[27]"The blood group system."
Reid M.E., Christine Lomas-Francis C.
(In) Reid M.E., Christine Lomas-Francis C. (eds.); The blood group antigen factsbook, pp.29-104, Academic Press, Oxford (2004)
Cited for: REVIEW, VARIANTS.
[28]"ABH blood group antigens in O-glycans of human glycophorin A."
Podbielska M., Fredriksson S.A., Nilsson B., Lisowska E., Krotkiewski H.
Arch. Biochem. Biophys. 429:145-153(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
[29]"Altered structure and anion transport properties of band 3 (AE1, SLC4A1) in human red cells lacking glycophorin A."
Bruce L.J., Pan R.J., Cope D.L., Uchikawa M., Gunn R.B., Cherry R.J., Tanner M.J.
J. Biol. Chem. 279:2414-2420(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[30]"Capsid region involved in hepatitis A virus binding to glycophorin A of the erythrocyte membrane."
Sanchez G., Aragones L., Costafreda M.I., Ribes E., Bosch A., Pinto R.M.
J. Virol. 78:9807-9813(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS RECEPTOR FOR FOR HEPATITIS A VIRUS.
[31]"Hsa, an adhesin of Streptococcus gordonii DL1, binds to alpha2-3-linked sialic acid on glycophorin A of the erythrocyte membrane."
Yajima A., Urano-Tashiro Y., Shimazu K., Takashima E., Takahashi Y., Konishi K.
Microbiol. Immunol. 52:69-77(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STREPTOCOCCUS GORDONII HSA PROTEIN.
[32]"Interaction of anion exchanger 1 and glycophorin A in human erythroleukaemic K562 cells."
Pang A.J., Reithmeier R.A.
Biochem. J. 421:345-356(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[33]"One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11.7 Tesla."
Dill K., Hu S.H., Berman E., Pavia A.A., Lacombe J.M.
J. Protein Chem. 9:129-136(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[34]"A transmembrane helix dimer: structure and implications."
Mackenzie K.R., Prestegard J.H., Engelman D.M.
Science 276:131-133(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 81-120.
[35]"Improved prediction for the structure of the dimeric transmembrane domain of glycophorin A obtained through global searching."
Adams P.D., Engelman D.M., Bruenger A.T.
Proteins 26:257-261(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 93-110.
[36]"Molecular basis for the human erythrocyte glycophorin specifying the Miltenberger class I (MiI) phenotype."
Huang C.-H., Spruell P., Moulds J.J., Blumenfeld O.O.
Blood 80:257-263(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ENEH/VW MET-47.
[37]"Molecular analysis of human glycophorin MiIX gene shows a silent segment transfer and untemplated mutation resulting from gene conversion via sequence repeats."
Huang C.H., Skov F., Daniels G., Tippett P., Blumenfeld O.O.
Blood 80:2379-2387(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ENEH/HUT ANTIGEN LYS-47.
[38]"Alteration of splice site selection by an exon mutation in the human glycophorin A gene."
Huang C.H., Reid M., Daniels G., Blumenfeld O.O.
J. Biol. Chem. 268:25902-25908(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ERIK ARG-78.
[39]"Glycophorin A mutation Ala65 --> Pro gives rise to a novel pair of MNS alleles ENEP (MNS39) and HAG (MNS41) and altered Wrb expression: direct evidence for GPA/band 3 interaction necessary for normal Wrb expression."
Poole J., Banks J., Bruce L.J., Ring S.M., Levene C., Stern H., Overbeeke M.A., Tanner M.J.
Transfus. Med. 9:167-174(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ENEP/HAG PRO-84.
[40]"The low-frequency MNS blood group antigens Ny(a) (MNS18) and Os(a) (MNS38) are associated with GPA amino acid substitutions."
Daniels G.L., Bruce L.J., Mawby W.J., Green C.A., Petty A., Okubo Y., Kornstad L., Tanner M.J.
Transfusion 40:555-559(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NY(A) GLU-46 AND OS(A) SER-73.
[41]"The MNS blood group antigens, Vr (MNS12) and Mt(a) (MNS14), each arise from an amino acid substitution on glycophorin A."
Storry J.R., Coghlan G., Poole J., Figueroa D., Reid M.E.
Vox Sang. 78:52-56(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VR TYR-66 AND MT(A) ILE-77.
+Additional computationally mapped references.

Web resources

dbRBC/BGMUT

Blood group antigen gene mutation database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M12857 mRNA. Translation: AAA88044.1.
X08054 mRNA. Translation: CAA30843.1.
M24128 expand/collapse EMBL AC list , M24123, M24134, M24124, M24126, M24127 Genomic DNA. Translation: AAA52768.1.
X51798 mRNA. Translation: CAA36095.1.
L31860 mRNA. Translation: AAA88051.1.
EU338231 mRNA. Translation: ACA96789.1.
EU338233 mRNA. Translation: ACA96791.1.
EU338234 mRNA. Translation: ACA96792.1.
GU347002 mRNA. Translation: ADU25340.1.
GU347003 mRNA. Translation: ADU25341.1.
AK290561 mRNA. Translation: BAF83250.1.
AC107223 Genomic DNA. No translation available.
BC005319 mRNA. Translation: AAH05319.1.
BC013328 mRNA. Translation: AAH13328.1.
M36281 mRNA. Translation: AAA52624.1. Different initiation.
CCDSCCDS34069.1. [P02724-1]
PIRA25131. A33931.
RefSeqNP_002090.4. NM_002099.6.
UniGeneHs.434973.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AFONMR-A/B81-120[»]
1MSRmodel-A/B93-110[»]
2KPENMR-A/B89-117[»]
2KPFNMR-A/B80-117[»]
ProteinModelPortalP02724.
SMRP02724. Positions 81-120.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000354003.

Chemistry

BindingDBP02724.
ChEMBLCHEMBL5806.

PTM databases

PhosphoSiteP02724.
UniCarbKBP02724.

Polymorphism databases

DMDM259016238.

Proteomic databases

PaxDbP02724.
PRIDEP02724.

Protocols and materials databases

DNASU2993.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000324022; ENSP00000324483; ENSG00000170180. [P02724-3]
ENST00000360771; ENSP00000354003; ENSG00000170180.
ENST00000535709; ENSP00000445398; ENSG00000170180. [P02724-2]
GeneID2993.
KEGGhsa:2993.

Organism-specific databases

CTD2993.
GeneCardsGC04M145030.
HGNCHGNC:4702. GYPA.
HPACAB002658.
HPA014811.
MIM111300. gene+phenotype.
611162. phenotype.
neXtProtNX_P02724.
PharmGKBPA29080.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG114778.
HOGENOMHOG000089933.
HOVERGENHBG005850.
InParanoidP02724.
KOK06575.
OrthoDBEOG7ZWD4D.
PhylomeDBP02724.
TreeFamTF338555.

Gene expression databases

ArrayExpressP02724.
BgeeP02724.
CleanExHS_GYPA.
GenevestigatorP02724.

Family and domain databases

InterProIPR001195. Glycophorin.
IPR018938. Glycophorin_CS.
[Graphical view]
PANTHERPTHR13813. PTHR13813. 1 hit.
PIRSFPIRSF002466. Glycophorin. 1 hit.
PROSITEPS00312. GLYCOPHORIN_A. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02724.
GeneWikiGYPA.
GenomeRNAi2993.
NextBio11862.
PROP02724.
SOURCESearch...

Entry information

Entry nameGLPA_HUMAN
AccessionPrimary (citable) accession number: P02724
Secondary accession number(s): A8K3E6 expand/collapse secondary AC list , B8Q182, B8Q185, Q9BS51
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 22, 2009
Last modified: July 9, 2014
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

Human cell differentiation molecules

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

Blood group antigen proteins

Nomenclature of blood group antigens and list of entries