P02724 (GLPA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycophorin-A

Alternative name(s):
MN sialoglycoprotein
PAS-2
Sialoglycoprotein alpha
CD_antigen=CD235a

Gene names

Name:	GYPA
Synonyms:	GPA

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	150 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.20 Ref.22 Ref.25 Ref.28 Ref.29 Ref.31
Subunit structure	Homodimer. Interacts with Streptococcus gordonii hsa protein. Ref.18 Ref.23 Ref.30
Subcellular location	Cell membrane; Single-pass type I membrane protein. Note: Appears to be colocalized with SLC4A1. Ref.24
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.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane Transmembrane helix
Ligand	Sialic acid
Molecular function	Blood group antigen Host cell receptor for virus entry Receptor
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cytoskeletal anchoring at plasma membrane Inferred from electronic annotation. Source: Compara regulation of response to osmotic stress Inferred from electronic annotation. Source: Compara virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	external side of plasma membrane Inferred from electronic annotation. Source: Compara integral to plasma membrane Inferred from electronic annotation. Source: Compara plasma membrane Traceable author statement Ref.37. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-702665,EBI-702665

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.10

Chain

20 – 150

131

Glycophorin-A

PRO_0000012134

Regions

Topological domain

20 – 91

72

Extracellular

Transmembrane

92 – 114

23

Helical

Topological domain

115 – 150

36

Cytoplasmic

Amino acid modifications

Glycosylation

21

1

O-linked (GalNAc...) Ref.10 Ref.19

Glycosylation

22

1

O-linked (GalNAc...) Ref.10 Ref.19

Glycosylation

23

1

O-linked (GalNAc...) Ref.10 Ref.19

Glycosylation

29

1

O-linked (GalNAc...) Ref.10 Ref.19

Glycosylation

30

1

O-linked (GalNAc...) Ref.10 Ref.19

Glycosylation

31

1

O-linked (GalNAc...) Ref.10 Ref.19

Glycosylation

32

1

O-linked (GalNAc...) Ref.10 Ref.19

Glycosylation

36

1

O-linked (GalNAc...) Ref.19

Glycosylation

38

1

O-linked (GalNAc...) Ref.19

Glycosylation

41

1

O-linked (GalNAc...) Ref.10 Ref.19

Glycosylation

44

1

O-linked (GalNAc...) Ref.10 Ref.19

Glycosylation

45

1

N-linked (GlcNAc...) Ref.10 Ref.19

Glycosylation

52

1

O-linked (GalNAc...) Ref.19

Glycosylation

56

1

O-linked (GalNAc...) Ref.10 Ref.19

Glycosylation

63

1

O-linked (GalNAc...) Ref.10 Ref.19

Glycosylation

66

1

O-linked (GalNAc...) Ref.10 Ref.19

Glycosylation

69

1

O-linked (GalNAc...) Ref.10 Ref.19

Natural variations

Natural variant

13

1

E → A. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8 Ref.9
Corresponds to variant rs4449373 [ dbSNP | Ensembl ].

VAR_058911

Natural variant

13

1

E → G.
Corresponds to variant rs4449373 [ dbSNP | Ensembl ].

VAR_059977

Natural variant

20

1

S → L in N antigen and M(g) antigen. Ref.2 Ref.7 Ref.8
Corresponds to variant rs7682260 [ dbSNP | Ensembl ].

VAR_003190

Natural variant

23

1

T → N in M(g) antigen. Ref.14

VAR_058912

Natural variant

24

1

G → D.
Corresponds to variant rs7658293 [ dbSNP | Ensembl ].

VAR_058913

Natural variant

24

1

G → E in N antigen, in M(c) antigen and in M(g) antigen. Ref.2 Ref.7 Ref.8 Ref.13
Corresponds to variant rs7687256 [ dbSNP | Ensembl ].

VAR_003191

Natural variant

46

1

D → E in Ny(a) antigen. Ref.39

VAR_058914

Natural variant

47

1

T → K in ENEH/Hut antigen. Ref.36

VAR_058915

Natural variant

47

1

T → M in ENEH/Vw antigen. Ref.35

VAR_058916

Natural variant

50

1

R → W in Or antigen.

VAR_058917

Natural variant

66

1

S → Y in Vr antigen. Ref.40
Corresponds to variant rs56077914 [ dbSNP | Ensembl ].

VAR_058918

Natural variant

73

1

P → S in Os(a) antigen. Ref.39

VAR_058919

Natural variant

76

1

E → K in Ri(a) antigen.

VAR_058920

Natural variant

77

1

T → I in Mt(a) antigen. Ref.40
Corresponds to variant rs56172553 [ dbSNP | Ensembl ].

VAR_058921

Natural variant

78

1

G → R in ERIK antigen. Ref.37
Corresponds to variant rs1800582 [ dbSNP | Ensembl ].

VAR_058922

Natural variant

82

1

Q → K in ENAV/MARS antigen.

VAR_058923

Natural variant

84

1

A → P in ENEP/HAG antigen. Ref.38

VAR_058924

Experimental info

Mutagenesis

87

1

F → C: Diminishes dimerization. Ref.25

Mutagenesis

88

1

S → C: Diminishes dimerization. Ref.25

Mutagenesis

90

1

P → C: Diminishes dimerization. Ref.25

Mutagenesis

91

1

E → C: Diminishes dimerization. Ref.25

Mutagenesis

94

1

L → I: Diminishes dimerization. Ref.22

Mutagenesis

95

1

I → A: Diminishes dimerization. Ref.22

Mutagenesis

98

1

G → L: Diminishes dimerization. Ref.22

Mutagenesis

102

1

G → L: Abolishes dimerization. Ref.22

Sequence conflict

30

1

S → T AA sequence Ref.10

Sequence conflict

36

1

T → S AA sequence Ref.10

Sequence conflict

133

1

T → R in AAA88044. Ref.1

Secondary structure

1

.

.

.

.

.

150

Helix Strand Turn

Details...

Beta strand

84 – 86

3

Helix

91 – 117

27

Sequences

	Sequence		Length	Mass (Da)
	P02724 [UniParc]. Last modified September 22, 2009. Version 2. Checksum: 48A5450E22FA99C9	FASTA	150	16,331
	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

References

	« Hide 'large scale' referencesShow '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], 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], 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], 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], VARIANT ALA-13. Tissue: Blood.
[6]	"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. , 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], VARIANT ALA-13. Tissue: Kidney.
[7]	"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. , 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.
[8]	"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 ALA-13, VARIANTS N LEU-20 AND GLU-24. Tissue: Bone marrow and Lung.
[9]	"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, VARIANT ALA-13.
[10]	"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.
[11]	Furthmayr H., Galardy R., Tomita M., Marchesi V.T. Submitted (JUN-1977) to the PIR data bank Cited for: SEQUENCE REVISION TO 81-120.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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).
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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, MASS SPECTROMETRY.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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.
[34]	"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.
[35]	"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.
[36]	"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.
[37]	"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.
[38]	"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.
[39]	"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.
[40]	"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 , M24123, M24134, M24124, M24126, M24127 Genomic DNA. Translation: AAA52768.1.
X51798 mRNA. Translation: CAA36095.1.
L31860 mRNA. Translation: AAA88051.1.
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.

IPI

IPI00298800.

PIR

A25131. A33931.

RefSeq

NP_002090.4. NM_002099.6.

UniGene

Hs.434973.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AFO	NMR	-	A/B	81-120	[»]
1MSR	model	-	A/B	93-110	[»]
2KPE	NMR	-	A/B	89-117	[»]
2KPF	NMR	-	A/B	80-117	[»]

ProteinModelPortal

P02724.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000354003.

PTM databases

GlycoSuiteDB

P02724.

PhosphoSite

P02724.

Polymorphism databases

DMDM

259016238.

Proteomic databases

PaxDb

P02724.

PRIDE

P02724.

Protocols and materials databases

DNASU

2993.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000360771; ENSP00000354003; ENSG00000170180.

GeneID

2993.

KEGG

hsa:2993.

Organism-specific databases

CTD

2993.

GeneCards

GC04M145030.

HGNC

HGNC:4702. GYPA.

HPA

CAB002658.
HPA014811.

MIM

111300. gene+phenotype.
611162. phenotype.

neXtProt

NX_P02724.

PharmGKB

PA29080.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG114778.

HOGENOM

HOG000089933.

HOVERGEN

HBG005850.

InParanoid

P02724.

KO

K06575.

OrthoDB

EOG4NP751.

Gene expression databases

ArrayExpress

P02724.

Bgee

P02724.

CleanEx

HS_GYPA.

Genevestigator

P02724.

GermOnline

ENSG00000170180. Homo sapiens.

Family and domain databases

InterPro

IPR001195. Glycophorin.
IPR018938. Glycophorin_CS.
[Graphical view]

PANTHER

PTHR13813. PTHR13813. 1 hit.

Pfam

PF01102. Glycophorin_A. 1 hit.
[Graphical view]

PIRSF

PIRSF002466. Glycophorin. 1 hit.

PROSITE

PS00312. GLYCOPHORIN_A. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P02724.

ChEMBL

CHEMBL5806.

EvolutionaryTrace

P02724.

GenomeRNAi

2993.

NextBio

11862.

SOURCE

Search...

Entry information

Entry name

GLPA_HUMAN

Accession

Primary (citable) accession number: P02724
Secondary accession number(s): A8K3E6, Q9BS51

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	September 22, 2009
Last modified:	May 1, 2013
This is version 146 of the entry and version 2 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.